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.


1mo2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1mo2.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1mo2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1mo2| PDB=1mo2 | SCENE= }}
{{STRUCTURE_1mo2| PDB=1mo2 | SCENE= }}
-
'''Thioesterase Domain from 6-Deoxyerythronolide Synthase (DEBS TE), pH 8.5'''
+
===Thioesterase Domain from 6-Deoxyerythronolide Synthase (DEBS TE), pH 8.5===
-
==Overview==
+
<!--
-
Modular polyketide synthases (PKSs) synthesize the polyketide cores of pharmacologically important natural products such as erythromycin and picromycin. Understanding PKSs at high resolution could present new opportunities for chemoenzymatic synthesis of complex molecules. The crystal structures of macrocycle-forming thioesterase (TE) domains from the picromycin synthase (PICS) and 6-deoxyerythronolide B synthase (DEBS) were determined to 1.8-3.0 A with an R(crys) of 19.2-24.4%, including three structures of PICS TE (crystallized at pH 7.6, 8.0, and 8.4) and a second crystal form of DEBS TE. As predicted by the previous work on DEBS TE [Tsai, S. C., et al. (2001) Proc. Natl. Acad. Sci. U.S.A. 98, 14808-14813], PICS TE contains an open substrate channel and a hydrophobic dimer interface. Notwithstanding their similarity, the dimer interfaces and substrate channels of DEBS TE and PICS TE reveal key differences. The structural basis for the divergent substrate specificities of DEBS TE and PICS TE is analyzed. The size of the substrate channel increases with increasing pH, presumably due to electrostatic repulsion in the channel at elevated pH. Together, these structures support previous predictions that macrocycle-forming thioesterases from PKSs share the same protein fold, an open substrate channel, a similar catalytic mechanism, and a hydrophobic dimer interface. They also provide a basis for the design of enzymes capable of catalyzing regioselective macrocyclization of natural or synthetic substrates. A series of high-resolution snapshots of a protein channel at different pHs is presented alongside analysis of channel residues, which could help in the redesign of the protein channel architecture.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12379102}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12379102 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12379102}}
==About this Structure==
==About this Structure==
Line 38: Line 42:
[[Category: Te]]
[[Category: Te]]
[[Category: Thioesterase]]
[[Category: Thioesterase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:29:44 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:31:18 2008''

Revision as of 21:31, 2 July 2008

Image:1mo2.png

Template:STRUCTURE 1mo2

Thioesterase Domain from 6-Deoxyerythronolide Synthase (DEBS TE), pH 8.5

Template:ABSTRACT PUBMED 12379102

About this Structure

1MO2 is a Single protein structure of sequence from Saccharopolyspora erythraea. Full crystallographic information is available from OCA.

Reference

Insights into channel architecture and substrate specificity from crystal structures of two macrocycle-forming thioesterases of modular polyketide synthases., Tsai SC, Lu H, Cane DE, Khosla C, Stroud RM, Biochemistry. 2002 Oct 22;41(42):12598-606. PMID:12379102

Page seeded by OCA on Thu Jul 3 00:31:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mo2"
Personal tools