1hm8
From Proteopedia
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'''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''' | ||
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[[Category: Peneff, C.]] | [[Category: Peneff, C.]] | ||
[[Category: Sulzenbacher, G.]] | [[Category: Sulzenbacher, G.]] | ||
| - | [[Category: | + | [[Category: Acetyltransferase]] |
| - | [[Category: | + | [[Category: Bifunctional]] |
| - | [[Category: | + | [[Category: Crystallography]] |
| - | [[Category: | + | [[Category: Domain-interchange]] |
| - | [[Category: | + | [[Category: Drug design]] |
| - | [[Category: | + | [[Category: Left-handed-beta-helix]] |
| - | [[Category: | + | [[Category: Pyrophosphorylase rossmann-like fold]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 16:00, 2 May 2008
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.
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 Fri May 2 19:00:29 2008
Categories: Single protein | Streptococcus pneumoniae | UDP-N-acetylglucosamine diphosphorylase | Bourne, Y. | Fassy, F. | Gal, L. | Peneff, C. | Sulzenbacher, G. | Acetyltransferase | Bifunctional | Crystallography | Domain-interchange | Drug design | Left-handed-beta-helix | Pyrophosphorylase rossmann-like fold | Trimer
