|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='4wes' size='340' side='right'caption='[[4wes]], [[Resolution|resolution]] 1.08Å' scene=''> | | <StructureSection load='4wes' size='340' side='right'caption='[[4wes]], [[Resolution|resolution]] 1.08Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wes]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WES OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WES FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wes]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_pasteurianum_DSM_525_=_ATCC_6013 Clostridium pasteurianum DSM 525 = ATCC 6013]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WES FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=ICS:IRON-SULFUR-MOLYBDENUM+CLUSTER+WITH+INTERSTITIAL+CARBON'>ICS</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.08Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1] </span></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=ICS:IRON-SULFUR-MOLYBDENUM+CLUSTER+WITH+INTERSTITIAL+CARBON'>ICS</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wes OCA], [http://pdbe.org/4wes PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wes RCSB], [http://www.ebi.ac.uk/pdbsum/4wes PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wes ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wes OCA], [https://pdbe.org/4wes PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wes RCSB], [https://www.ebi.ac.uk/pdbsum/4wes PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wes ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NIFD_CLOPA NIFD_CLOPA]] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. [[http://www.uniprot.org/uniprot/NIFK_CLOPA NIFK_CLOPA]] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. | + | [https://www.uniprot.org/uniprot/NIFD_CLOPA NIFD_CLOPA] This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 26: |
Line 26: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Clostridium pasteurianum]] | + | [[Category: Clostridium pasteurianum DSM 525 = ATCC 6013]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nitrogenase]]
| + | [[Category: Kaiser JT]] |
| - | [[Category: Kaiser, J T]] | + | [[Category: Morrison CN]] |
| - | [[Category: Morrison, C N]] | + | [[Category: Rees DC]] |
| - | [[Category: Rees, D C]] | + | [[Category: Zhang LM]] |
| - | [[Category: Zhang, L M]] | + | |
| - | [[Category: Nitrogen fixation]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
4wes is a 4 chain structure with sequence from Clostridium pasteurianum DSM 525 = ATCC 6013. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.08Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
NIFD_CLOPA This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
Publication Abstract from PubMed
The X-ray crystal structure of the nitrogenase MoFe protein from Clostridium pasteurianum (Cp1) has been determined at 1.08 A 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 alpha-subunit and a deletion in the beta-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 alpha-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.
Nitrogenase MoFe protein from Clostridium pasteurianum at 1.08 A resolution: comparison with the Azotobacter vinelandii MoFe protein.,Zhang LM, Morrison CN, Kaiser JT, Rees DC Acta Crystallogr D Biol Crystallogr. 2015 Feb;71(Pt 2):274-82. doi:, 10.1107/S1399004714025243. Epub 2015 Jan 23. PMID:25664737[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhang LM, Morrison CN, Kaiser JT, Rees DC. Nitrogenase MoFe protein from Clostridium pasteurianum at 1.08 A resolution: comparison with the Azotobacter vinelandii MoFe protein. Acta Crystallogr D Biol Crystallogr. 2015 Feb;71(Pt 2):274-82. doi:, 10.1107/S1399004714025243. Epub 2015 Jan 23. PMID:25664737 doi:http://dx.doi.org/10.1107/S1399004714025243
|
