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1wow

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Revision as of 16:22, 11 April 2018

Crystal structure of heme oxygenase-2 from Synechocystis sp. PCC 6803 complexed with heme in ferrous form

Structural highlights

1wow is a 2 chain structure with sequence from Aphanocapsa sp. (strain n-1). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1wov, 1wox
Activity:	Heme oxygenase, with EC number 1.14.99.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HO2_SYNY3] Catalyzes the opening of the heme ring with the release of iron. Key enzyme in the synthesis of the chromophoric part of the photosynthetic antennae (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 PubMed

Phycobiliproteins, light-harvesting proteins in cyanobacteria, red algae, and cryptophytes, contain phycobilin pigments. Phycobilins are synthesized from biliverdin, which is produced by the oxidative cleavage of the heme porphyrin ring catalyzed by heme oxygenase (HO). Two paralogs of ho (ho1 and ho2) have been identified in the genome of the cyanobacterium, Synechocystis sp. PCC 6803. The recombinant proteins of both paralogs (Syn HO-1 and Syn HO-2) possess in vitro heme degradation activity. We have determined the crystal structures of Syn HO-2 in complex with heme (heme-Syn HO-2) and its reduced and NO bound forms. The heme-Syn HO-2 crystal was a nonmerohedral twin, and detwinned diffraction data were used to refine the structure. Although heme-Syn HO-2 shares common folding with other HOs, the C-terminal segment is ordered and turns back to the heme-binding side. Gel-filtration chromatography analysis and molecular packing in the crystal indicate that heme-Syn HO-2 forms a homodimer, in which the C-terminal ordered segments interact with each other. Because Syn HO-2 is a monomer in the apo state, the dimeric interaction may aid in the selection of the reducing partner but likely does not interfere with heme binding. The heme iron is coordinated by a water molecule in the ferric form, but the distal water is absent in the ferrous form. In all of the Syn HO-2 structures, several water molecules form a hydrogen-bond network at the distal hemepocket, which is involved in HO activity. Upon NO binding, the side-chain conformation of Tyr 156 changes. Tyr 156 is located at the hydrophobic cluster, which interrupts the possible H(+) pathway from the molecular surface to the hemepocket. Thus, Tyr 156 may function as a H(+) shuttle by changing conformation.

Crystal structure of dimeric heme oxygenase-2 from Synechocystis sp. PCC 6803 in complex with heme.,Sugishima M, Hagiwara Y, Zhang X, Yoshida T, Migita CT, Fukuyama K Biochemistry. 2005 Mar 22;44(11):4257-66. PMID:15766254^[1]

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

References

↑ Sugishima M, Hagiwara Y, Zhang X, Yoshida T, Migita CT, Fukuyama K. Crystal structure of dimeric heme oxygenase-2 from Synechocystis sp. PCC 6803 in complex with heme. Biochemistry. 2005 Mar 22;44(11):4257-66. PMID:15766254 doi:http://dx.doi.org/10.1021/bi0480483

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Crystal structure of heme oxygenase-2 from Synechocystis sp. PCC 6803 complexed with heme in ferrous form==
 <StructureSection load='1wow' size='340' side='right' caption='[[1wow]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wov|1wov]], [[1wox|1wox]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </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=1wow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wow OCA], [http://pdbe.org/1wow PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wow RCSB], [http://www.ebi.ac.uk/pdbsum/1wow 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=1wow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wow OCA], [http://pdbe.org/1wow PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wow RCSB], [http://www.ebi.ac.uk/pdbsum/1wow PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wow ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wo/1wow_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wo/1wow_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 32: / Line 33: @@
 ==See Also==
 *[[Heme oxygenase|Heme oxygenase]]
+*[[User:Eric Martz/Entertaining PDB codes|User:Eric Martz/Entertaining PDB codes]]
 == References ==
 <references/>

1wow

From Proteopedia

Revision as of 16:22, 11 April 2018

Crystal structure of heme oxygenase-2 from Synechocystis sp. PCC 6803 complexed with heme in ferrous form

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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