1k5s: Difference between revisions

Revision as of 09:50, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1k5s.png

Template:STRUCTURE 1k5s

PENICILLIN ACYLASE, MUTANT COMPLEXED WITH PPAPENICILLIN ACYLASE, MUTANT COMPLEXED WITH PPA

Template:ABSTRACT PUBMED 15254299

About this StructureAbout this Structure

1K5S is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structural and kinetic studies on ligand binding in wild-type and active-site mutants of penicillin acylase., Alkema WB, Hensgens CM, Snijder HJ, Keizer E, Dijkstra BW, Janssen DB, Protein Eng Des Sel. 2004 May;17(5):473-80. Epub 2004 Jul 14. PMID:15254299

Page seeded by OCA on Wed Jul 2 09:49:59 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1k5s.jpg|left|200px]]
+{{Seed}}
+[[Image:1k5s.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1k5s|  PDB=1k5s  |  SCENE=  }}
-'''PENICILLIN ACYLASE, MUTANT COMPLEXED WITH PPA'''
+===PENICILLIN ACYLASE, MUTANT COMPLEXED WITH PPA===
-==Overview==
+<!--
-Penicillin acylase catalyses the condensation of Calpha-substituted phenylacetic acids with beta-lactam nucleophiles, producing semi-synthetic beta-lactam antibiotics. For efficient synthesis a low affinity for phenylacetic acid and a high affinity for Calpha-substituted phenylacetic acid derivatives is desirable. We made three active site mutants, alphaF146Y, betaF24A and alphaF146Y/betaF24A, which all had a 2- to 10-fold higher affinity for Calpha-substituted compounds than wild-type enzyme. In addition, betaF24A had a 20-fold reduced affinity for phenylacetic acid. The molecular basis of the improved properties was investigated by X-ray crystallography. These studies showed that the higher affinity of alphaF146Y for (R)-alpha-methylphenylacetic acid can be explained by van der Waals interactions between alphaY146:OH and the Calpha-substituent. The betaF24A mutation causes an opening of the phenylacetic acid binding site. Only (R)-alpha-methylphenylacetic acid, but not phenylacetic acid, induces a conformation with the ligand tightly bound, explaining the weak binding of phenylacetic acid. A comparison of the betaF24A structure with other open conformations of penicillin acylase showed that betaF24 has a fixed position, whereas alphaF146 acts as a flexible lid on the binding site and reorients its position to achieve optimal substrate binding.
+The line below this paragraph, {{ABSTRACT_PUBMED_15254299}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15254299 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15254299}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Helice]]
 [[Category: Ntn-hydrolase fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:20:50 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 09:49:59 2008''