From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1e3d.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1e3d.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1e3d| PDB=1e3d | SCENE= }} | | {{STRUCTURE_1e3d| PDB=1e3d | SCENE= }} |
| | | | |
| - | '''[NIFE] HYDROGENASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774'''
| + | ===[NIFE] HYDROGENASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The primary and three-dimensional structures of a [NiFe] hydrogenase isolated from D. desulfitricans ATCC 27774 were determined, by nucleotide analysis and single-crystal X-ray crystallography. The three-dimensional structural model was refined to R=0.167 and Rfree=0.223 using data to 1.8 A resolution. Two unique structural features are observed: the [4Fe-4S] cluster nearest the [NiFe] centre has been modified [4Fe-3S-3O] by loss of one sulfur atom and inclusion of three oxygen atoms; a three-fold disorder was observed for Cys536 which binds to the nickel atom in the [NiFe] centre. Also, the bridging sulfur atom that caps the active site was found to have partial occupancy, thus corresponding to a partly activated enzyme. These structural features may have biological relevance. In particular, the two less-populated rotamers of Cys536 may be involved in the activation process of the enzyme, as well as in the catalytic cycle. Molecular modelling studies were carried out on the interaction between this [NiFe] hydrogenase and its physiological partner, the tetrahaem cytochrome c3 from the same organism. The lowest energy docking solutions were found to correspond to an interaction between the haem IV region in tetrahaem cytochrome c3 with the distal [4Fe-4S] cluster in [NiFe] hydrogenase. This interaction should correspond to efficient electron transfer and be physiologically relevant, given the proximity of the two redox centres and the fact that electron transfer decay coupling calculations show high coupling values and a short electron transfer pathway. On the other hand, other docking solutions have been found that, despite showing low electron transfer efficiency, may give clues on possible proton transfer mechanisms between the two molecules.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11191224}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11191224 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_11191224}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 33: |
Line 37: |
| | [[Category: Hydrogenase]] | | [[Category: Hydrogenase]] |
| | [[Category: Molecular modelling]] | | [[Category: Molecular modelling]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:36:35 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:05:01 2008'' |
Revision as of 21:05, 30 June 2008
Template:STRUCTURE 1e3d
[NIFE] HYDROGENASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774
Template:ABSTRACT PUBMED 11191224
About this Structure
1E3D is a Protein complex structure of sequences from Desulfovibrio desulfuricans. Full crystallographic information is available from OCA.
Reference
[NiFe] hydrogenase from Desulfovibrio desulfuricans ATCC 27774: gene sequencing, three-dimensional structure determination and refinement at 1.8 A and modelling studies of its interaction with the tetrahaem cytochrome c3., Matias PM, Soares CM, Saraiva LM, Coelho R, Morais J, Le Gall J, Carrondo MA, J Biol Inorg Chem. 2001 Jan;6(1):63-81. PMID:11191224
Page seeded by OCA on Tue Jul 1 00:05:01 2008
