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.
1hm0
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1hm0.gif|left|200px]] | + | [[Image:1hm0.gif|left|200px]] |
| - | + | ||
| - | '''CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE, GLMU''' | + | {{Structure |
| + | |PDB= 1hm0 |SIZE=350|CAPTION= <scene name='initialview01'>1hm0</scene>, resolution 2.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_diphosphorylase UDP-N-acetylglucosamine diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.23 2.7.7.23] | ||
| + | |GENE= GLMU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 Streptococcus pneumoniae]) | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE, GLMU''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1HM0 is a [ | + | 1HM0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HM0 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11118459 11118459] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptococcus pneumoniae]] | [[Category: Streptococcus pneumoniae]] | ||
| Line 25: | Line 34: | ||
[[Category: trimer]] | [[Category: trimer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:38:49 2008'' |
Revision as of 09:38, 20 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | GLMU (Streptococcus pneumoniae) | ||||||
| Activity: | UDP-N-acetylglucosamine diphosphorylase, with EC number 2.7.7.23 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Thu Mar 20 11:38:49 2008
