2b4k: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2b4k]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Acetobacter_pasteurianus Acetobacter pasteurianus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B4K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2B4K FirstGlance]. <br> | <table><tr><td colspan='2'>[[2b4k]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Acetobacter_pasteurianus Acetobacter pasteurianus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B4K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2B4K FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG9:D-PHENYLGLYCINE'>PG9</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG9:D-PHENYLGLYCINE'>PG9</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aehA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=438 Acetobacter pasteurianus])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aehA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=438 Acetobacter pasteurianus])</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-amino-acid_esterase Alpha-amino-acid esterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.43 3.1.1.43] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-amino-acid_esterase Alpha-amino-acid esterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.43 3.1.1.43] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b4k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2b4k RCSB], [http://www.ebi.ac.uk/pdbsum/2b4k PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b4k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2b4k RCSB], [http://www.ebi.ac.uk/pdbsum/2b4k PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 32: | Line 32: | ||
[[Category: Acetobacter pasteurianus]] | [[Category: Acetobacter pasteurianus]] | ||
[[Category: Alpha-amino-acid esterase]] | [[Category: Alpha-amino-acid esterase]] | ||
[[Category: Barends, T R.M | [[Category: Barends, T R.M]] | ||
[[Category: Dijkstra, B W | [[Category: Dijkstra, B W]] | ||
[[Category: Janssen, D B | [[Category: Janssen, D B]] | ||
[[Category: Jekel, P A | [[Category: Jekel, P A]] | ||
[[Category: Polderman-Tijmes, J J | [[Category: Polderman-Tijmes, J J]] | ||
[[Category: Williams, C | [[Category: Williams, C]] | ||
[[Category: Wybenga, G | [[Category: Wybenga, G]] | ||
[[Category: Alpha-beta hydrolase]] | [[Category: Alpha-beta hydrolase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 13:05, 8 January 2015
Acetobacter turbidans alpha-amino acid ester hydrolase complexed with phenylglycineAcetobacter turbidans alpha-amino acid ester hydrolase complexed with phenylglycine
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe alpha-amino acid ester hydrolase (AEH) from Acetobacter turbidans is a bacterial enzyme catalyzing the hydrolysis and synthesis of beta-lactam antibiotics. The crystal structures of the native enzyme, both unliganded and in complex with the hydrolysis product D-phenylglycine are reported, as well as the structures of an inactive mutant (S205A) complexed with the substrate ampicillin, and an active site mutant (Y206A) with an increased tendency to catalyze antibiotic production rather than hydrolysis. The structure of the native enzyme shows an acyl binding pocket, in which D-phenylglycine binds, and an additional space that is large enough to accommodate the beta-lactam moiety of an antibiotic. In the S205A mutant, ampicillin binds in this pocket in a non-productive manner, making extensive contacts with the side chain of Tyr(112), which also participates in oxyanion hole formation. In the Y206A mutant, the Tyr(112) side chain has moved with its hydroxyl group toward the catalytic serine. Because this changes the properties of the beta-lactam binding site, this could explain the increased beta-lactam transferase activity of this mutant. Acetobacter turbidans alpha-amino acid ester hydrolase: how a single mutation improves an antibiotic-producing enzyme.,Barends TR, Polderman-Tijmes JJ, Jekel PA, Williams C, Wybenga G, Janssen DB, Dijkstra BW J Biol Chem. 2006 Mar 3;281(9):5804-10. Epub 2005 Dec 23. PMID:16377627[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||