1gjn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1gjn.gif|left|200px]]<br /><applet load="1gjn" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1gjn.gif|left|200px]]
-
caption="1gjn, resolution 1.35&Aring;" />
+
 
-
'''HYDROGEN PEROXIDE DERIVED MYOGLOBIN COMPOUND II AT PH 5.2'''<br />
+
{{Structure
 +
|PDB= 1gjn |SIZE=350|CAPTION= <scene name='initialview01'>1gjn</scene>, resolution 1.35&Aring;
 +
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene>
 +
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=HYD:HYDROXY GROUP'>HYD</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''HYDROGEN PEROXIDE DERIVED MYOGLOBIN COMPOUND II AT PH 5.2'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1GJN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=HYD:'>HYD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJN OCA].
+
1GJN is a [[Single protein]] structure of sequence from [http://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].
==Reference==
==Reference==
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11935353 11935353]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/11935353 11935353]
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 29: Line 38:
[[Category: reaction intermediate]]
[[Category: reaction intermediate]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:50:47 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:24:02 2008''

Revision as of 09:24, 20 March 2008

Image:1gjn.gif


PDB ID 1gjn

Drag the structure with the mouse to rotate
, resolution 1.35Å
Sites:
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



HYDROGEN PEROXIDE DERIVED MYOGLOBIN COMPOUND II AT PH 5.2


Overview

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.

About this Structure

1GJN is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Thu Mar 20 11:24:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gjn"
Personal tools