1hm0
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(New page: 200px<br /><applet load="1hm0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hm0, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 14:31, 20 November 2007
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CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE, GLMU
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
1HM0 is a Single protein structure of sequence from Streptococcus pneumoniae with CA as ligand. Active as UDP-N-acetylglucosamine diphosphorylase, with EC number 2.7.7.23 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
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