1qdb: Difference between revisions

Revision as of 16:16, 28 July 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:1qdb.png

Template:STRUCTURE 1qdb

CYTOCHROME C NITRITE REDUCTASECYTOCHROME C NITRITE REDUCTASE

Template:ABSTRACT PUBMED 10440380

About this StructureAbout this Structure

1QDB is a Single protein structure of sequence from Sulfurospirillum deleyianum. Full crystallographic information is available from OCA.

ReferenceReference

Structure of cytochrome c nitrite reductase., Einsle O, Messerschmidt A, Stach P, Bourenkov GP, Bartunik HD, Huber R, Kroneck PM, Nature. 1999 Jul 29;400(6743):476-80. PMID:10440380

Page seeded by OCA on Mon Jul 28 16:16:06 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1qdb.jpg|left|200px]]
+{{Seed}}
+[[Image:1qdb.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1qdb|  PDB=1qdb  |  SCENE=  }}
-'''CYTOCHROME C NITRITE REDUCTASE'''
+===CYTOCHROME C NITRITE REDUCTASE===
-==Overview==
+<!--
-The enzyme cytochrome c nitrite reductase catalyses the six-electron reduction of nitrite to ammonia as one of the key steps in the biological nitrogen cycle, where it participates in the anaerobic energy metabolism of dissimilatory nitrate ammonification. Here we report on the crystal structure of this enzyme from the microorganism Sulfurospirillum deleyianum, which we solved by multiwavelength anomalous dispersion methods. We propose a reaction scheme for the transformation of nitrite based on structural and spectroscopic information. Cytochrome c nitrite reductase is a functional dimer, with 10 close-packed haem groups of type c and an unusual lysine-coordinated high-spin haem at the active site. By comparing the haem arrangement of this nitrite reductase with that of other multihaem cytochromes, we have been able to identify a family of proteins in which the orientation of haem groups is conserved whereas structure and function are not.
+The line below this paragraph, {{ABSTRACT_PUBMED_10440380}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10440380 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10440380}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: C-type cytochrome lysine-coordinated heme nitrite reductase]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:09:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:16:06 2008''