1q9j
From Proteopedia
(New page: 200px<br /><applet load="1q9j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q9j, resolution 2.75Å" /> '''Structure of polyket...) |
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| - | [[Image:1q9j.gif|left|200px]]<br /><applet load="1q9j" size=" | + | [[Image:1q9j.gif|left|200px]]<br /><applet load="1q9j" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1q9j, resolution 2.75Å" /> | caption="1q9j, resolution 2.75Å" /> | ||
'''Structure of polyketide synthase associated protein 5 from Mycobacterium tuberculosis'''<br /> | '''Structure of polyketide synthase associated protein 5 from Mycobacterium tuberculosis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Polyketide-associated protein A5 (PapA5) is an acyltransferase that is | + | Polyketide-associated protein A5 (PapA5) is an acyltransferase that is involved in production of phthiocerol and phthiodiolone dimycocerosate esters, a class of virulence-enhancing lipids produced by Mycobacterium tuberculosis. Structural analysis of PapA5 at 2.75-A resolution reveals a two-domain structure that shares unexpected similarity to structures of chloramphenicol acetyltransferase, dihydrolipoyl transacetylase, carnitine acetyltransferase, and VibH, a non-ribosomal peptide synthesis condensation enzyme. The PapA5 active site includes conserved histidine and aspartic acid residues that are critical to PapA5 acyltransferase activity. PapA5 catalyzes acyl transfer reactions on model substrates that contain long aliphatic carbon chains, and two hydrophobic channels were observed linking the PapA5 surface to the active site with properties consistent with these biochemical activities and substrate preferences. An additional alpha helix not observed in other acyltransferase structures blocks the putative entrance into the PapA5 active site, indicating that conformational changes may be associated with PapA5 activity. PapA5 represents the first structure solved for a protein involved in polyketide synthesis in Mycobacteria. |
==About this Structure== | ==About this Structure== | ||
| - | 1Q9J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http:// | + | 1Q9J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q9J OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Buglino, J.]] | [[Category: Buglino, J.]] | ||
| - | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
| - | [[Category: Lima, C | + | [[Category: Lima, C D.]] |
| - | [[Category: NYSGXRC, New | + | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] |
| - | [[Category: Onwueme, K | + | [[Category: Onwueme, K C.]] |
| - | [[Category: Quadri, L | + | [[Category: Quadri, L E.]] |
[[Category: new york structural genomix research consortium]] | [[Category: new york structural genomix research consortium]] | ||
[[Category: nysgxrc]] | [[Category: nysgxrc]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:23 2008'' |
Revision as of 12:37, 21 February 2008
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Structure of polyketide synthase associated protein 5 from Mycobacterium tuberculosis
Overview
Polyketide-associated protein A5 (PapA5) is an acyltransferase that is involved in production of phthiocerol and phthiodiolone dimycocerosate esters, a class of virulence-enhancing lipids produced by Mycobacterium tuberculosis. Structural analysis of PapA5 at 2.75-A resolution reveals a two-domain structure that shares unexpected similarity to structures of chloramphenicol acetyltransferase, dihydrolipoyl transacetylase, carnitine acetyltransferase, and VibH, a non-ribosomal peptide synthesis condensation enzyme. The PapA5 active site includes conserved histidine and aspartic acid residues that are critical to PapA5 acyltransferase activity. PapA5 catalyzes acyl transfer reactions on model substrates that contain long aliphatic carbon chains, and two hydrophobic channels were observed linking the PapA5 surface to the active site with properties consistent with these biochemical activities and substrate preferences. An additional alpha helix not observed in other acyltransferase structures blocks the putative entrance into the PapA5 active site, indicating that conformational changes may be associated with PapA5 activity. PapA5 represents the first structure solved for a protein involved in polyketide synthesis in Mycobacteria.
About this Structure
1Q9J is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
Crystal structure of PapA5, a phthiocerol dimycocerosyl transferase from Mycobacterium tuberculosis., Buglino J, Onwueme KC, Ferreras JA, Quadri LE, Lima CD, J Biol Chem. 2004 Jul 16;279(29):30634-42. Epub 2004 May 3. PMID:15123643
Page seeded by OCA on Thu Feb 21 14:37:23 2008
Categories: Mycobacterium tuberculosis | Single protein | Buglino, J. | Burley, S K. | Lima, C D. | NYSGXRC, New York Structural GenomiX Research Consortium. | Onwueme, K C. | Quadri, L E. | New york structural genomix research consortium | Nysgxrc | Polyketide synthase associated protein; conjugating enzyme papa5; mycobacterium tuberculosis | Protein structure initiative | Psi | Structural genomics
