1gjn

From Proteopedia

(Difference between revisions)

Current revision

Hydrogen Peroxide Derived Myoglobin Compound II at pH 5.2

Structural highlights

1gjn is a 1 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.35Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MYG_HORSE Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.

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 biological conversions of O(2) and peroxides to water as well as certain incorporations of oxygen atoms into small organic molecules can be catalyzed by metal ions in different clusters or cofactors. The catalytic cycle of these reactions passes through similar metal-based complexes in which one oxygen- or peroxide-derived oxygen atom is coordinated to an oxidized form of the catalytic metal center. In haem-based peroxidases or oxygenases the ferryl (Fe(IV)O) form is important in compound I and compound II, which are two and one oxidation equivalents higher than the ferric (Fe(III)) form, respectively. In this study we report the 1.35 A structure of a compound II model protein, obtained by reacting hydrogen peroxide with ferric myoglobin at pH 5.2. The molecular geometry is virtually unchanged compared to the ferric form, indicating that these reactive intermediates do not undergo large structural changes. It is further suggested that at low pH the dominating compound II resonance form is a hydroxyl radical ferric iron rather than an oxo-ferryl form, based on the short hydrogen bonding to the distal histidine (2.70 A) and the Fe...O distance. The 1.92 A Fe...O distance is in agreement with an EXAFS study of compound II in horseradish peroxidase.

An iron hydroxide moiety in the 1.35 A resolution structure of hydrogen peroxide derived myoglobin compound II at pH 5.2.,Hersleth HP, Dalhus B, Gorbitz CH, Andersson KK J Biol Inorg Chem. 2002 Mar;7(3):299-304. Epub 2001 Oct 11. PMID:11935353^[1]

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

References

↑ Hersleth HP, Dalhus B, Gorbitz CH, Andersson KK. An iron hydroxide moiety in the 1.35 A resolution structure of hydrogen peroxide derived myoglobin compound II at pH 5.2. J Biol Inorg Chem. 2002 Mar;7(3):299-304. Epub 2001 Oct 11. PMID:11935353 doi:10.1007/s007750100296

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/1gjn"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1gjn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GJN FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1azi|1azi]], [[1bje|1bje]], [[1dwr|1dwr]], [[1dws|1dws]], [[1dwt|1dwt]], [[1hrm|1hrm]], [[1hsy|1hsy]], [[1rse|1rse]], [[1wla|1wla]], [[1xch|1xch]], [[1yma|1yma]], [[1ymb|1ymb]], [[1ymc|1ymc]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1gjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjn OCA], [https://pdbe.org/1gjn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gjn RCSB], [https://www.ebi.ac.uk/pdbsum/1gjn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gjn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
+[https://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 38: / Line 38: @@
 [[Category: Equus caballus]]
 [[Category: Large Structures]]
-[[Category: Andersson, K K]]
+[[Category: Andersson KK]]
-[[Category: Dalhus, B]]
+[[Category: Dalhus B]]
-[[Category: Gorbitz, C H]]
+[[Category: Gorbitz CH]]
-[[Category: Hersleth, H P]]
+[[Category: Hersleth H-P]]
-[[Category: Ferryl]]
-[[Category: Haem]]
-[[Category: Heme]]
-[[Category: Hydroxy radical]]
-[[Category: Monooxygenase]]
-[[Category: Oxygen activation]]
-[[Category: Oxygen transport]]
-[[Category: Peroxidase]]
-[[Category: Reaction intermediate]]

1gjn

From Proteopedia

Current revision

Hydrogen Peroxide Derived Myoglobin Compound II at pH 5.2

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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