This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2rdz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2rdz.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2rdz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2rdz| PDB=2rdz | SCENE= }}
{{STRUCTURE_2rdz| PDB=2rdz | SCENE= }}
-
'''High Resolution Crystal Structure of the Escherichia coli Cytochrome c Nitrite Reductase.'''
+
===High Resolution Crystal Structure of the Escherichia coli Cytochrome c Nitrite Reductase.===
-
==Overview==
+
<!--
-
The pentaheme cytochrome c nitrite reductase (NrfA) of Escherichia coli is responsible for nitrite reduction during anaerobic respiration when nitrate is scarce. The NrfA active site consists of a hexacoordinate high-spin heme with a lysine ligand on the proximal side and water/hydroxide or substrate on the distal side. There are four further highly conserved active site residues including a glutamine (Q263) positioned 8 A from the heme iron for which the side chain, unusually, coordinates a conserved, essential calcium ion. Mutation of this glutamine to the more usual calcium ligand, glutamate, results in an increase in the K m for nitrite by around 10-fold, while V max is unaltered. Protein film voltammetry showed that lower potentials were required to detect activity from NrfA Q263E when compared with native enzyme, consistent with the introduction of a negative charge into the vicinity of the active site heme. EPR and MCD spectroscopic studies revealed the high spin state of the active site to be preserved, indicating that a water/hydroxide molecule is still coordinated to the heme in the resting state of the enzyme. Comparison of the X-ray crystal structures of the as-prepared, oxidized native and mutant enzymes showed an increased bond distance between the active site heme Fe(III) iron and the distal ligand in the latter as well as changes to the structure and mobility of the active site water molecule network. These results suggest that an important function of the unusual Q263-calcium ion pair is to increase substrate affinity through its role in supporting a network of hydrogen bonded water molecules stabilizing the active site heme distal ligand.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18311941}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18311941 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18311941}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Reductase]]
[[Category: Reductase]]
[[Category: Transport]]
[[Category: Transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:43:19 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:26:19 2008''

Revision as of 08:26, 29 July 2008

Image:2rdz.png

Template:STRUCTURE 2rdz

High Resolution Crystal Structure of the Escherichia coli Cytochrome c Nitrite Reductase.

Template:ABSTRACT PUBMED 18311941

About this Structure

2RDZ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Role of a Conserved Glutamine Residue in Tuning the Catalytic Activity of Escherichia coli Cytochrome c Nitrite Reductase., Clarke TA, Kemp GL, Wonderen JH, Doyle RM, Cole JA, Tovell N, Cheesman MR, Butt JN, Richardson DJ, Hemmings AM, Biochemistry. 2008 Mar 25;47(12):3789-3799. Epub 2008 Mar 1. PMID:18311941

Page seeded by OCA on Tue Jul 29 11:26:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rdz"
Personal tools