1ted

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{{STRUCTURE_1ted| PDB=1ted | SCENE= }}
{{STRUCTURE_1ted| PDB=1ted | SCENE= }}
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'''Crystal structure of a type III polyketide synthase PKS18 from Mycobacterium tuberculosis'''
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===Crystal structure of a type III polyketide synthase PKS18 from Mycobacterium tuberculosis===
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==Overview==
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The superfamily of plant and bacterial type III polyketide synthases (PKSs) produces diverse metabolites with distinct biological functions. PKS18, a type III PKS from Mycobacterium tuberculosis, displays an unusual broad specificity for aliphatic long-chain acyl-coenzyme A (acyl-CoA) starter units (C(6)-C(20)) to produce tri- and tetraketide pyrones. The crystal structure of PKS18 reveals a 20 A substrate binding tunnel, hitherto unidentified in this superfamily of enzymes. This remarkable tunnel extends from the active site to the surface of the protein and is primarily generated by subtle changes of backbone dihedral angles in the core of the protein. Mutagenic studies combined with structure determination provide molecular insights into the structural elements that contribute to the chain length specificity of the enzyme. This first bacterial type III PKS structure underlines a fascinating example of the way in which subtle changes in protein architecture can generate metabolite diversity in nature.
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(as it appears on PubMed at http://www.pubmed.gov), where 15286723 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15286723}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
A novel tunnel in mycobacterial type III polyketide synthase reveals the structural basis for generating diverse metabolites., Sankaranarayanan R, Saxena P, Marathe UB, Gokhale RS, Shanmugam VM, Rukmini R, Nat Struct Mol Biol. 2004 Sep;11(9):894-900. Epub 2004 Aug 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15286723 15286723]
A novel tunnel in mycobacterial type III polyketide synthase reveals the structural basis for generating diverse metabolites., Sankaranarayanan R, Saxena P, Marathe UB, Gokhale RS, Shanmugam VM, Rukmini R, Nat Struct Mol Biol. 2004 Sep;11(9):894-900. Epub 2004 Aug 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15286723 15286723]
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Crystallization and preliminary X-ray crystallographic investigations of an unusual type III polyketide synthase PKS18 from Mycobacterium tuberculosis., Rukmini R, Shanmugam VM, Saxena P, Gokhale RS, Sankaranarayanan R, Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):749-51. Epub 2004, Mar 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15039574 15039574]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Naringenin-chalcone synthase]]
[[Category: Naringenin-chalcone synthase]]
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[[Category: Substrate binding tunnel]]
[[Category: Substrate binding tunnel]]
[[Category: Thiolase fold]]
[[Category: Thiolase fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:51:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:00:24 2008''

Revision as of 21:00, 28 July 2008

Image:1ted.png

Template:STRUCTURE 1ted

Crystal structure of a type III polyketide synthase PKS18 from Mycobacterium tuberculosis

Template:ABSTRACT PUBMED 15286723

About this Structure

1TED is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

A novel tunnel in mycobacterial type III polyketide synthase reveals the structural basis for generating diverse metabolites., Sankaranarayanan R, Saxena P, Marathe UB, Gokhale RS, Shanmugam VM, Rukmini R, Nat Struct Mol Biol. 2004 Sep;11(9):894-900. Epub 2004 Aug 1. PMID:15286723

Crystallization and preliminary X-ray crystallographic investigations of an unusual type III polyketide synthase PKS18 from Mycobacterium tuberculosis., Rukmini R, Shanmugam VM, Saxena P, Gokhale RS, Sankaranarayanan R, Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):749-51. Epub 2004, Mar 23. PMID:15039574

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