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.


1hm8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hm8.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1hm8.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hm8| PDB=1hm8 | SCENE= }}
{{STRUCTURE_1hm8| PDB=1hm8 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE, GLMU, BOUND TO ACETYL COENZYME A'''
+
===CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE, GLMU, BOUND TO ACETYL COENZYME A===
-
==Overview==
+
<!--
-
The bifunctional bacterial enzyme N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU) catalyzes the two-step formation of UDP-GlcNAc, a fundamental precursor in bacterial cell wall biosynthesis. With the emergence of new resistance mechanisms against beta-lactam and glycopeptide antibiotics, the biosynthetic pathway of UDP-GlcNAc represents an attractive target for drug design of new antibacterial agents. The crystal structures of Streptococcus pneumoniae GlmU in unbound form, in complex with acetyl-coenzyme A (AcCoA) and in complex with both AcCoA and the end product UDP-GlcNAc, have been determined and refined to 2.3, 2.5, and 1.75 A, respectively. The S. pneumoniae GlmU molecule is organized in two separate domains connected via a long alpha-helical linker and associates as a trimer, with the 50-A-long left-handed beta-helix (LbetaH) C-terminal domains packed against each other in a parallel fashion and the C-terminal region extended far away from the LbetaH core and exchanged with the beta-helix from a neighboring subunit in the trimer. AcCoA binding induces the formation of a long and narrow tunnel, enclosed between two adjacent LbetaH domains and the interchanged C-terminal region of the third subunit, giving rise to an original active site architecture at the junction of three subunits.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11118459}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11118459 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11118459}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Pyrophosphorylase rossmann-like fold]]
[[Category: Pyrophosphorylase rossmann-like fold]]
[[Category: Trimer]]
[[Category: Trimer]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:00:29 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:23:23 2008''

Revision as of 05:23, 1 July 2008

Image:1hm8.png

Template:STRUCTURE 1hm8

CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE, GLMU, BOUND TO ACETYL COENZYME A

Template:ABSTRACT PUBMED 11118459

About this Structure

1HM8 is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.

Reference

Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture., Sulzenbacher G, Gal L, Peneff C, Fassy F, Bourne Y, J Biol Chem. 2001 Apr 13;276(15):11844-51. Epub 2000 Dec 15. PMID:11118459

Page seeded by OCA on Tue Jul 1 08:23:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hm8"
Personal tools