1gnl

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(Difference between revisions)

Revision as of 00:01, 9 February 2016

Hybrid Cluster Protein from Desulfovibrio desulfuricans ATCC 27774 X-ray structure at 1.25A resolution using synchrotron radiation at a wavelength of 0.933A

Structural highlights

1gnl is a 2 chain structure with sequence from Desulfovibrio desulfuricans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1gn9
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[HCP_DESDA] Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O (By similarity).[HAMAP-Rule:MF_00069]

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 PubMed

The structures of the hybrid cluster proteins (HCPs) from the sulfate-reducing bacteria Desulfovibrio desulfuricans (ATCC 27774) and Desulfovibrio vulgaris (Hildenborough) have been elucidated at a resolution of 1.25 A using X-ray synchrotron radiation techniques. In the case of the D. desulfuricans protein, protein isolation, purification, crystallization and X-ray data collection were carried out under strict anaerobic conditions, whereas for the D. vulgaris protein the conditions were aerobic. However, both structures are essentially the same, comprising three domains and two iron-sulfur centres. One of these centres situated near the exterior of the molecules in domain 1 is a cubane [4Fe-4S] cluster, whereas the other, located at the interface of the three domains, contains the unusual four-iron cluster initially found in the D. vulgaris protein. Details of the structures and the associated EPR spectroscopy of the D. desulfuricans protein are reported herein. These structures show that the nature of the hybrid cluster, containing both oxygen and sulfur bridges, is independent of the presence of oxygen in the isolation and crystallization procedure and also does not vary significantly with changes in the oxidation state. The structures and amino acid sequences of the HCP are compared with the recently elucidated structure of the catalytic subunit of a carbon monoxide dehydrogenase from Carboxydothermus hydrogenoformans and related dehydrogenases. Electronic supplementary material to this paper can be obtained by using the Springer Link server located at http://dx.doi.org/10.1007/s00775-001-0326-y.

Hybrid cluster proteins (HCPs) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at 1.25 A resolution using synchrotron radiation.,Macedo S, Mitchell EP, Romao CV, Cooper SJ, Coelho R, Liu MY, Xavier AV, LeGall J, Bailey S, Garner DC, Hagen WR, Teixeira M, Carrondo MA, Lindley P J Biol Inorg Chem. 2002 Apr;7(4-5):514-25. Epub 2002 Jan 23. PMID:11941509^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Macedo S, Mitchell EP, Romao CV, Cooper SJ, Coelho R, Liu MY, Xavier AV, LeGall J, Bailey S, Garner DC, Hagen WR, Teixeira M, Carrondo MA, Lindley P. Hybrid cluster proteins (HCPs) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at 1.25 A resolution using synchrotron radiation. J Biol Inorg Chem. 2002 Apr;7(4-5):514-25. Epub 2002 Jan 23. PMID:11941509 doi:10.1007/s00775-001-0326-y

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gnl"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gn9|1gn9]]</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=1gnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gnl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gnl RCSB], [http://www.ebi.ac.uk/pdbsum/1gnl PDBsum]</span></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=1gnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gnl OCA], [http://pdbe.org/1gnl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gnl RCSB], [http://www.ebi.ac.uk/pdbsum/1gnl PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 17: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gnl ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1gnl" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1gnl

From Proteopedia

Revision as of 00:01, 9 February 2016

Hybrid Cluster Protein from Desulfovibrio desulfuricans ATCC 27774 X-ray structure at 1.25A resolution using synchrotron radiation at a wavelength of 0.933A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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