From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1e2u.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1e2u.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1e2u| PDB=1e2u | SCENE= }} | | {{STRUCTURE_1e2u| PDB=1e2u | SCENE= }} |
| | | | |
| - | '''LOW TEMPERATURE STUCTURE OF HYBRID CLUSTER PROTEIN FROM DESULFOVIBRIO VULGARIS TO 1.6A'''
| + | ===LOW TEMPERATURE STUCTURE OF HYBRID CLUSTER PROTEIN FROM DESULFOVIBRIO VULGARIS TO 1.6A=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The three-dimensional structure of the hybrid cluster protein from Desulfovibrio vulgaris (Hildenborough) has been determined at 1.6 A resolution using synchrotron X-ray radiation. The protein can be divided into three domains: an N-terminal mainly alpha-helical domain and two similar domains comprising a central beta-sheet flanked by alpha-helices. The protein contains two 4Fe clusters with an edge-to-edge distance of 10.9 A. Four cysteine residues at the N-terminus of the protein are ligands to the iron atoms of a conventional [4Fe-4S] cubane cluster. The second cluster has an unusual asymmetric structure and has been named the hybrid cluster to reflect the variety of protein ligands, namely two mu-sulfido bridges, two mu(2)-oxo bridges, and a further disordered bridging ligand. Anomalous differences in data collected at 1.488 A and close to the iron edge at 1.743 A have been used to confirm the identity of the metal and sulfur atoms. The hybrid cluster is buried in the center of the protein, but is accessible through a large hydrophobic cavity that runs the length of domain 3. Hydrophobic channels have previously been identified as access routes to the active centers in redox enzymes with gaseous substrates. The hybrid cluster is also accessible by a hydrophilic channel. The [4Fe-4S] cubane cluster is close to an indentation on the surface of the protein and can also be approached on the opposite side by a long solvent channel. At the present time, neither the significance of these channels nor, indeed, the function of the hybrid cluster protein is known.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11106482}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11106482 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_11106482}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 31: |
Line 35: |
| | [[Category: Iron sulfur]] | | [[Category: Iron sulfur]] |
| | [[Category: Prismane]] | | [[Category: Prismane]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:35:27 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:03:12 2008'' |
Revision as of 21:03, 30 June 2008
Template:STRUCTURE 1e2u
LOW TEMPERATURE STUCTURE OF HYBRID CLUSTER PROTEIN FROM DESULFOVIBRIO VULGARIS TO 1.6A
Template:ABSTRACT PUBMED 11106482
About this Structure
1E2U is a Single protein structure of sequence from Desulfovibrio vulgaris. Full crystallographic information is available from OCA.
Reference
Hybrid-cluster protein (HCP) from Desulfovibrio vulgaris (Hildenborough) at 1.6 A resolution., Cooper SJ, Garner CD, Hagen WR, Lindley PF, Bailey S, Biochemistry. 2000 Dec 12;39(49):15044-54. PMID:11106482
Page seeded by OCA on Tue Jul 1 00:03:12 2008
