1hm8: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
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

File: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 "https://proteopedia.org/index.php?title=1hm8&oldid=607751"