1e2u: Difference between revisions
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<StructureSection load='1e2u' size='340' side='right'caption='[[1e2u]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1e2u' size='340' side='right'caption='[[1e2u]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1e2u]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1e2u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E2U FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=FSO:IRON/SULFUR/OXYGEN+HYBRID+CLUSTER'>FSO</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></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=1e2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e2u OCA], [https://pdbe.org/1e2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e2u RCSB], [https://www.ebi.ac.uk/pdbsum/1e2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e2u ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/HCP_DESVH HCP_DESVH] Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Desulfovibrio vulgaris]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bailey | [[Category: Bailey S]] | ||
[[Category: Cooper | [[Category: Cooper SJ]] | ||
[[Category: Hagen | [[Category: Hagen WR]] | ||
[[Category: Lindley | [[Category: Lindley PF]] | ||
Latest revision as of 11:10, 6 December 2023
Low Temperature Structure of Hybrid Cluster Protein from Desulfovibrio vulgaris to 1.6ALow Temperature Structure of Hybrid Cluster Protein from Desulfovibrio vulgaris to 1.6A
Structural highlights
FunctionHCP_DESVH Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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