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.


1x7g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1x7g.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1x7g.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1x7g| PDB=1x7g | SCENE= }}
{{STRUCTURE_1x7g| PDB=1x7g | SCENE= }}
-
'''Actinorhodin Polyketide Ketoreductase, act KR, with NADP bound'''
+
===Actinorhodin Polyketide Ketoreductase, act KR, with NADP bound===
-
==Overview==
+
<!--
-
Aromatic polyketides are a class of natural products that include many pharmaceutically important aromatic compounds. Understanding the structure and function of PKS will provide clues to the molecular basis of polyketide biosynthesis specificity. Polyketide chain reduction by ketoreductase (KR) provides regio- and stereochemical diversity. Two cocrystal structures of actinorhodin polyketide ketoreductase (act KR) were solved to 2.3 A with either the cofactor NADP(+) or NADPH bound. The monomer fold is a highly conserved Rossmann fold. Subtle differences between structures of act KR and fatty acid KRs fine-tune the tetramer interface and substrate binding pocket. Comparisons of the NADP(+)- and NADPH-bound structures indicate that the alpha6-alpha7 loop region is highly flexible. The intricate proton-relay network in the active site leads to the proposed catalytic mechanism involving four waters, NADPH, and the active site tetrad Asn114-Ser144-Tyr157-Lys161. Acyl carrier protein and substrate docking models shed light on the molecular basis of KR regio- and stereoselectivity, as well as the differences between aromatic polyketide and fatty acid biosyntheses. Sequence comparison indicates that the above features are highly conserved among aromatic polyketide KRs. The structures of act KR provide an important step toward understanding aromatic PKS and will enhance our ability to design novel aromatic polyketide natural products with different reduction patterns.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15544323}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15544323 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15544323}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Polyketide]]
[[Category: Polyketide]]
[[Category: Short chain dehydrogenase/reductase]]
[[Category: Short chain dehydrogenase/reductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:39:54 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:19:11 2008''

Revision as of 17:19, 27 July 2008

Image:1x7g.png

Template:STRUCTURE 1x7g

Actinorhodin Polyketide Ketoreductase, act KR, with NADP bound

Template:ABSTRACT PUBMED 15544323

About this Structure

1X7G is a Single protein structure of sequence from Streptomyces coelicolor. Full crystallographic information is available from OCA.

Reference

Structural analysis of actinorhodin polyketide ketoreductase: cofactor binding and substrate specificity., Korman TP, Hill JA, Vu TN, Tsai SC, Biochemistry. 2004 Nov 23;43(46):14529-38. PMID:15544323

Page seeded by OCA on Sun Jul 27 20:19:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1x7g"
Personal tools