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.


1w3p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1w3p.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1w3p.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1w3p| PDB=1w3p | SCENE= }}
{{STRUCTURE_1w3p| PDB=1w3p | SCENE= }}
-
'''NIMA FROM D. RADIODURANS WITH A HIS71-PYRUVATE RESIDUE'''
+
===NIMA FROM D. RADIODURANS WITH A HIS71-PYRUVATE RESIDUE===
-
==Overview==
+
<!--
-
5-Nitroimidazole-based antibiotics are compounds extensively used for treating infections in humans and animals caused by several important pathogens. They are administered as prodrugs, and their activation depends upon an anaerobic 1-electron reduction of the nitro group by a reduction pathway in the cells. Bacterial resistance toward these drugs is thought to be caused by decreased drug uptake and/or an altered reduction efficiency. One class of resistant strains, identified in Bacteroides, has been shown to carry Nim genes (NimA, -B, -C, -D, and -E), which encode for reductases that convert the nitro group on the antibiotic into a non-bactericidal amine. In this paper, we have described the crystal structure of NimA from Deinococcus radiodurans (drNimA) at 1.6 A resolution. We have shown that drNimA is a homodimer in which each monomer adopts a beta-barrel fold. We have identified the catalytically important His-71 along with the cofactor pyruvate and antibiotic binding sites, all of which are found at the monomer-monomer interface. We have reported three additional crystal structures of drNimA, one in which the antibiotic metronidazole is bound to the protein, one with pyruvate covalently bound to His-71, and one with lactate covalently bound to His-71. Based on these structures, a reaction mechanism has been proposed in which the 2-electron reduction of the antibiotic prevents accumulation of the toxic nitro radical. This mechanism suggests that Nim proteins form a new class of reductases, conferring resistance against 5-nitroimidazole-based antibiotics.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15492014}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15492014 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15492014}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Deinococcus radioduran]]
[[Category: Deinococcus radioduran]]
[[Category: Nim gene]]
[[Category: Nim gene]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:06:57 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:01:05 2008''

Revision as of 02:01, 29 July 2008

Template:STRUCTURE 1w3p

NIMA FROM D. RADIODURANS WITH A HIS71-PYRUVATE RESIDUE

Template:ABSTRACT PUBMED 15492014

About this Structure

1W3P is a Single protein structure of sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA.

Reference

Structural basis of 5-nitroimidazole antibiotic resistance: the crystal structure of NimA from Deinococcus radiodurans., Leiros HK, Kozielski-Stuhrmann S, Kapp U, Terradot L, Leonard GA, McSweeney SM, J Biol Chem. 2004 Dec 31;279(53):55840-9. Epub 2004 Oct 18. PMID:15492014

Page seeded by OCA on Tue Jul 29 05:01:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools