1upx

From Proteopedia

(Difference between revisions)

Revision as of 06:55, 29 March 2023

The crystal structure of the Hybrid Cluster Protein from Desulfovibrio desulfuricans containing molecules in the oxidized and reduced states.

Structural highlights

1upx 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:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 hybrid cluster protein (HCP) from the sulfate-reducing bacteria Desulfovibrio desulfuricans ATCC 27774 has been isolated and crystallized anaerobically. The protein sample used in the crystallization studies was several months old, having been stored at 193 K, and initial crystal structure studies were unable to fully resolve details of the hybrid cluster despite the use of high-resolution data to 1.25 A collected at the ESRF, Grenoble, France. Full elucidation of the structure has only become possible with the complete knowledge of the as-isolated and fully reduced crystal structures. The analysis clarifies the significant movements in the position of the Fe atom linked to the persulfide moiety in the oxidized as-isolated protein and the S atom of the persulfide itself as the protein is reduced. The structures of the as-isolated and reduced states are discussed in terms of the putative function of the HCP proteins.

Structure of the hybrid cluster protein (HCP) from Desulfovibrio desulfuricans ATCC 27774 containing molecules in the oxidized and reduced states.,Macedo S, Aragao D, Mitchell EP, Lindley P Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2065-71. Epub 2003, Nov 27. PMID:14646063^[1]

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

References

↑ Macedo S, Aragao D, Mitchell EP, Lindley P. Structure of the hybrid cluster protein (HCP) from Desulfovibrio desulfuricans ATCC 27774 containing molecules in the oxidized and reduced states. Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2065-71. Epub 2003, Nov 27. PMID:14646063

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/1upx"

@@ Line 3: / Line 3: @@
 <StructureSection load='1upx' size='340' side='right'caption='[[1upx]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1upx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UPX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1UPX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1upx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UPX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UPX FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FSO:IRON/SULFUR/OXYGEN+HYBRID+CLUSTER'>FSO</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SF3:FE4-S3+CLUSTER'>SF3</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"><div style='overflow: auto; max-height: 3em;'>[[1gn9|1gn9]], [[1gnl|1gnl]], [[1oa0|1oa0]]</div></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=1upx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1upx OCA], [https://pdbe.org/1upx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1upx RCSB], [https://www.ebi.ac.uk/pdbsum/1upx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1upx ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1upx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1upx OCA], [http://pdbe.org/1upx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1upx RCSB], [http://www.ebi.ac.uk/pdbsum/1upx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1upx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HCP_DESDA HCP_DESDA]] Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O (By similarity).[HAMAP-Rule:MF_00069]
+[https://www.uniprot.org/uniprot/HCP_DESDA HCP_DESDA] Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O (By similarity).[HAMAP-Rule:MF_00069]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 34: @@
 [[Category: Desulfovibrio desulfuricans]]
 [[Category: Large Structures]]
-[[Category: Aragao, D]]
+[[Category: Aragao D]]
-[[Category: Lindley, P F]]
+[[Category: Lindley PF]]
-[[Category: Macedo, S]]
+[[Category: Macedo S]]
-[[Category: Mitchell, E P]]
+[[Category: Mitchell EP]]
-[[Category: Hybrid cluster]]
-[[Category: Oxidized iron-sulfur]]
-[[Category: Oxidoreductase]]
-[[Category: Reduced iron-sulfur]]

1upx

From Proteopedia

Revision as of 06:55, 29 March 2023

The crystal structure of the Hybrid Cluster Protein from Desulfovibrio desulfuricans containing molecules in the oxidized and reduced states.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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