2f98

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2f98.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2f98.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2f98| PDB=2f98 | SCENE= }}
{{STRUCTURE_2f98| PDB=2f98 | SCENE= }}
-
'''Crystal structure of the polyketide cyclase AknH with bound substrate and product analogue: implications for catalytic mechanism and product stereoselectivity.'''
+
===Crystal structure of the polyketide cyclase AknH with bound substrate and product analogue: implications for catalytic mechanism and product stereoselectivity.===
-
==Overview==
+
<!--
-
AknH is a small polyketide cyclase that catalyses the closure of the fourth carbon ring in aclacinomycin biosynthesis in Streptomyces galilaeus, converting aklanonic acid methyl ester to aklaviketone. The crystal structure analysis of this enzyme, in complex with substrate and product analogue, showed that it is closely related in fold and mechanism to the polyketide cyclase SnoaL that catalyses the corresponding reaction in the biosynthesis of nogalamycin. Similarity is also apparent at a functional level as AknH can convert nogalonic acid methyl ester, the natural substrate of SnoaL, to auraviketone in vitro and in constructs in vivo. Despite the conserved structural and mechanistic features between these enzymes, the reaction products of AknH and SnoaL are stereochemically distinct. Supplied with the same substrate, AknH yields a C9-R product, like most members of this family of polyketide cyclases, whereas the product of SnoaL has the opposite C9-S stereochemistry. A comparison of high-resolution crystal structures of the two enzymes combined with in vitro mutagenesis studies revealed two critical amino acid substitutions in the active sites, which contribute to product stereoselectivity in AknH. Replacement of residues Tyr15 and Asn51 of AknH, located in the vicinity of the main catalytic residue Asp121, by their SnoaL counter-parts phenylalanine and leucine, respectively, results in a complete loss of product stereoselectivity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16414075}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16414075 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16414075}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Polyketide cyclase]]
[[Category: Polyketide cyclase]]
[[Category: Stereoselectivity]]
[[Category: Stereoselectivity]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:37:01 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:45:36 2008''

Revision as of 23:45, 28 July 2008

Image:2f98.png

Template:STRUCTURE 2f98

Crystal structure of the polyketide cyclase AknH with bound substrate and product analogue: implications for catalytic mechanism and product stereoselectivity.

Template:ABSTRACT PUBMED 16414075

About this Structure

2F98 is a Single protein structure of sequence from Streptomyces galilaeus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the polyketide cyclase AknH with bound substrate and product analogue: implications for catalytic mechanism and product stereoselectivity., Kallio P, Sultana A, Niemi J, Mantsala P, Schneider G, J Mol Biol. 2006 Mar 17;357(1):210-20. Epub 2006 Jan 6. PMID:16414075

Page seeded by OCA on Tue Jul 29 02:45:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2f98"
Personal tools