Nitrogenase MoFe protein from Clostridium pasteurianum at 1.08Å resolution

Comparison with the Azotobacter vinelandii MoFe protein

Limei Zhang, Christine N. Morrison, Jens T. Kaiser, Douglas C. Rees

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

The X-ray crystal structure of the nitrogenase MoFe protein from Clostridium pasteurianum (Cp1) has been determined at 1.08Å resolution by multiwavelength anomalous diffraction phasing. Cp1 and the ortholog from Azotobacter vinelandii (Av1) represent two distinct families of nitrogenases, differing primarily by a long insertion in the -subunit and a deletion in the β-subunit of Cp1 relative to Av1. Comparison of these two MoFe protein structures at atomic resolution reveals conserved structural arrangements that are significant to the function of nitrogenase. The FeMo cofactors defining the active sites of the MoFe protein are essentially identical between the two proteins. The surrounding environment is also highly conserved, suggesting that this structural arrangement is crucial for nitrogen reduction. The P clusters are likewise similar, although the surrounding protein and solvent environment is less conserved relative to that of the FeMo cofactor. The P cluster and FeMo cofactor in Av1 and Cp1 are connected through a conserved water tunnel surrounded by similar secondary-structure elements. The long -subunit insertion loop occludes the presumed Fe protein docking surface on Cp1 with few contacts to the remainder of the protein. This makes it plausible that this loop is repositioned to open up the Fe protein docking surface for complex formation.

Original languageEnglish (US)
Pages (from-to)274-282
Number of pages9
JournalActa Crystallographica Section D: Biological Crystallography
Volume71
DOIs
StatePublished - Feb 1 2015

Fingerprint

Molybdoferredoxin
Azotobacter vinelandii
Nitrogenase
Clostridium
Membrane Proteins
Proteins
Catalytic Domain
Nitrogen
X-Rays
Water

Keywords

  • FeMo cofactor
  • P cluster
  • iron-sulfur clusters
  • metalloproteins

ASJC Scopus subject areas

  • Structural Biology

Cite this

Nitrogenase MoFe protein from Clostridium pasteurianum at 1.08Å resolution : Comparison with the Azotobacter vinelandii MoFe protein. / Zhang, Limei; Morrison, Christine N.; Kaiser, Jens T.; Rees, Douglas C.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 71, 01.02.2015, p. 274-282.

Research output: Contribution to journalArticle

@article{d77271a765a24ebfb42ef9ca9747462e,
title = "Nitrogenase MoFe protein from Clostridium pasteurianum at 1.08{\AA} resolution: Comparison with the Azotobacter vinelandii MoFe protein",
abstract = "The X-ray crystal structure of the nitrogenase MoFe protein from Clostridium pasteurianum (Cp1) has been determined at 1.08{\AA} resolution by multiwavelength anomalous diffraction phasing. Cp1 and the ortholog from Azotobacter vinelandii (Av1) represent two distinct families of nitrogenases, differing primarily by a long insertion in the -subunit and a deletion in the β-subunit of Cp1 relative to Av1. Comparison of these two MoFe protein structures at atomic resolution reveals conserved structural arrangements that are significant to the function of nitrogenase. The FeMo cofactors defining the active sites of the MoFe protein are essentially identical between the two proteins. The surrounding environment is also highly conserved, suggesting that this structural arrangement is crucial for nitrogen reduction. The P clusters are likewise similar, although the surrounding protein and solvent environment is less conserved relative to that of the FeMo cofactor. The P cluster and FeMo cofactor in Av1 and Cp1 are connected through a conserved water tunnel surrounded by similar secondary-structure elements. The long -subunit insertion loop occludes the presumed Fe protein docking surface on Cp1 with few contacts to the remainder of the protein. This makes it plausible that this loop is repositioned to open up the Fe protein docking surface for complex formation.",
keywords = "FeMo cofactor, P cluster, iron-sulfur clusters, metalloproteins",
author = "Limei Zhang and Morrison, {Christine N.} and Kaiser, {Jens T.} and Rees, {Douglas C.}",
year = "2015",
month = "2",
day = "1",
doi = "10.1107/S1399004714025243",
language = "English (US)",
volume = "71",
pages = "274--282",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "0907-4449",
publisher = "John Wiley and Sons Inc.",

}

TY - JOUR

T1 - Nitrogenase MoFe protein from Clostridium pasteurianum at 1.08Å resolution

T2 - Comparison with the Azotobacter vinelandii MoFe protein

AU - Zhang, Limei

AU - Morrison, Christine N.

AU - Kaiser, Jens T.

AU - Rees, Douglas C.

PY - 2015/2/1

Y1 - 2015/2/1

N2 - The X-ray crystal structure of the nitrogenase MoFe protein from Clostridium pasteurianum (Cp1) has been determined at 1.08Å resolution by multiwavelength anomalous diffraction phasing. Cp1 and the ortholog from Azotobacter vinelandii (Av1) represent two distinct families of nitrogenases, differing primarily by a long insertion in the -subunit and a deletion in the β-subunit of Cp1 relative to Av1. Comparison of these two MoFe protein structures at atomic resolution reveals conserved structural arrangements that are significant to the function of nitrogenase. The FeMo cofactors defining the active sites of the MoFe protein are essentially identical between the two proteins. The surrounding environment is also highly conserved, suggesting that this structural arrangement is crucial for nitrogen reduction. The P clusters are likewise similar, although the surrounding protein and solvent environment is less conserved relative to that of the FeMo cofactor. The P cluster and FeMo cofactor in Av1 and Cp1 are connected through a conserved water tunnel surrounded by similar secondary-structure elements. The long -subunit insertion loop occludes the presumed Fe protein docking surface on Cp1 with few contacts to the remainder of the protein. This makes it plausible that this loop is repositioned to open up the Fe protein docking surface for complex formation.

AB - The X-ray crystal structure of the nitrogenase MoFe protein from Clostridium pasteurianum (Cp1) has been determined at 1.08Å resolution by multiwavelength anomalous diffraction phasing. Cp1 and the ortholog from Azotobacter vinelandii (Av1) represent two distinct families of nitrogenases, differing primarily by a long insertion in the -subunit and a deletion in the β-subunit of Cp1 relative to Av1. Comparison of these two MoFe protein structures at atomic resolution reveals conserved structural arrangements that are significant to the function of nitrogenase. The FeMo cofactors defining the active sites of the MoFe protein are essentially identical between the two proteins. The surrounding environment is also highly conserved, suggesting that this structural arrangement is crucial for nitrogen reduction. The P clusters are likewise similar, although the surrounding protein and solvent environment is less conserved relative to that of the FeMo cofactor. The P cluster and FeMo cofactor in Av1 and Cp1 are connected through a conserved water tunnel surrounded by similar secondary-structure elements. The long -subunit insertion loop occludes the presumed Fe protein docking surface on Cp1 with few contacts to the remainder of the protein. This makes it plausible that this loop is repositioned to open up the Fe protein docking surface for complex formation.

KW - FeMo cofactor

KW - P cluster

KW - iron-sulfur clusters

KW - metalloproteins

UR - http://www.scopus.com/inward/record.url?scp=84922665432&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84922665432&partnerID=8YFLogxK

U2 - 10.1107/S1399004714025243

DO - 10.1107/S1399004714025243

M3 - Article

VL - 71

SP - 274

EP - 282

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 0907-4449

ER -