1q3g: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1q3g |SIZE=350|CAPTION= <scene name='initialview01'>1q3g</scene>, resolution 2.65Å | |PDB= 1q3g |SIZE=350|CAPTION= <scene name='initialview01'>1q3g</scene>, resolution 2.65Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=UDA:3 | |LIGAND= <scene name='pdbligand=UDA:3'-1-CARBOXY-1-PHOSPHONOOXY-ETHOXY-URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UDA</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_1-carboxyvinyltransferase UDP-N-acetylglucosamine 1-carboxyvinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.7 2.5.1.7] | |ACTIVITY= [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_1-carboxyvinyltransferase UDP-N-acetylglucosamine 1-carboxyvinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.7 2.5.1.7] | ||
|GENE= MURA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=550 Enterobacter cloacae]) | |GENE= MURA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=550 Enterobacter cloacae]) | ||
| Line 31: | Line 31: | ||
[[Category: inside-out alpha-beta barrel]] | [[Category: inside-out alpha-beta barrel]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:17:23 2008'' | ||
Revision as of 11:17, 23 March 2008
| |||||||||||||
| 1q3g, resolution 2.65Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | UDA and EDO | ||||||||||||
| Gene: | MURA (Enterobacter cloacae) | ||||||||||||
| Activity: | UDP-N-acetylglucosamine 1-carboxyvinyltransferase, with EC number 2.5.1.7 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
MurA (Asp305Ala) liganded with tetrahedral reaction intermediate
Overview
UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) constitute the small enzyme family of enolpyruvyl transferases, which catalyze the chemically unusual reaction of enolpyruvyl transfer. MurA catalyzes the first step in the biosynthesis of the bacterial cell wall; AroA is the sixth enzyme of the shikimate pathway leading to the synthesis of aromatic compounds in numerous microorganisms and plants. Because both metabolic pathways are absent from mammals but essential for the growth of microorganisms, MurA and AroA are attractive targets for the development of novel antimicrobial drugs. We have determined the x-ray structures of the D305A mutant of Enterobacter cloacae MurA and the D313A mutant of Escherichia coli AroA, both of which crystallized in the presence of their substrates. The structures depict the tetrahedral reaction intermediate states of the enzymes and prove that, without the aspartate side chain, the overall addition-elimination reaction in both enzymes is halted after the addition step. The presented structures lead to a new view of the catalytic mechanism and, moreover, provide an ideal starting point for the rational design of potent inhibitors of MurA and AroA.
About this Structure
1Q3G is a Single protein structure of sequence from Enterobacter cloacae. Full crystallographic information is available from OCA.
Reference
A new view of the mechanisms of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) derived from X-ray structures of their tetrahedral reaction intermediate states., Eschenburg S, Kabsch W, Healy ML, Schonbrunn E, J Biol Chem. 2003 Dec 5;278(49):49215-22. Epub 2003 Sep 16. PMID:13129913
Page seeded by OCA on Sun Mar 23 13:17:23 2008
