1aoq: Difference between revisions

Revision as of 17:18, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1aoq.png

Template:STRUCTURE 1aoq

CYTOCHROME CD1 NITRITE REDUCTASE WITH SUBSTRATE AND PRODUCT BOUNDCYTOCHROME CD1 NITRITE REDUCTASE WITH SUBSTRATE AND PRODUCT BOUND

Template:ABSTRACT PUBMED 9311786

About this StructureAbout this Structure

1AOQ is a Single protein structure of sequence from Paracoccus pantotrophus. Full crystallographic information is available from OCA.

ReferenceReference

Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme., Williams PA, Fulop V, Garman EF, Saunders NF, Ferguson SJ, Hajdu J, Nature. 1997 Sep 25;389(6649):406-12. PMID:9311786

Page seeded by OCA on Mon Jun 30 17:18:28 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1aoq.jpg|left|200px]]
+{{Seed}}
+[[Image:1aoq.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1aoq|  PDB=1aoq  |  SCENE=  }}
-'''CYTOCHROME CD1 NITRITE REDUCTASE WITH SUBSTRATE AND PRODUCT BOUND'''
+===CYTOCHROME CD1 NITRITE REDUCTASE WITH SUBSTRATE AND PRODUCT BOUND===
-==Overview==
+<!--
-Cytochrome cd1 nitrite reductase catalyses the conversion of nitrite to nitric oxide in the nitrogen cycle. The crystal structure of the oxidized enzyme shows that the d1 haem iron of the active site is ligated by His/Tyr side chains, and the c haem iron is ligated by a His/His ligand pair. Here we show that both haems undergo re-ligation during catalysis. Upon reduction, the tyrosine ligand of the d1 haem is released to allow substrate binding. Concomitantly, a refolding of the cytochrome c domain takes place, resulting in an unexpected change of the c haem iron coordination from His 17/His 69 to Met106/His69. This step is similar to the last steps in the folding of cytochrome c. The changes must affect the redox potential of the haems, and suggest a mechanism by which internal electron transfer is regulated. Structures of reaction intermediates show how nitric oxide is formed and expelled from the active-site iron, as well as how both haems return to their starting coordination. These results show how redox energy can be switched into conformational energy within a haem protein.
+The line below this paragraph, {{ABSTRACT_PUBMED_9311786}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9311786 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9311786}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Nitrite reductase]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:31:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:18:28 2008''