1oy0
From Proteopedia
(New page: 200px<br /><applet load="1oy0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oy0, resolution 2.80Å" /> '''The crystal Structur...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1oy0.gif|left|200px]]<br /><applet load="1oy0" size=" | + | [[Image:1oy0.gif|left|200px]]<br /><applet load="1oy0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1oy0, resolution 2.80Å" /> | caption="1oy0, resolution 2.80Å" /> | ||
'''The crystal Structure of the First Enzyme of Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase from Mycobacterium Tuberculosis Shows a Decameric Assembly and Terminal Helix-Swapping'''<br /> | '''The crystal Structure of the First Enzyme of Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase from Mycobacterium Tuberculosis Shows a Decameric Assembly and Terminal Helix-Swapping'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ketopantoate hydroxymethyltransferase (KPHMT) catalyzes the first | + | Ketopantoate hydroxymethyltransferase (KPHMT) catalyzes the first committed step in the biosynthesis of pantothenate, which is a precursor to coenzyme A and is required for penicillin biosynthesis. The crystal structure of KPHMT from Mycobacterium tuberculosis was determined by the single anomalous substitution (SAS) method at 2.8 A resolution. KPHMT adopts a structure that is a variation on the (beta/alpha) barrel fold, with a metal binding site proximal to the presumed catalytic site. The protein forms a decameric complex, with subunits in opposing pentameric rings held together by a swapping of their C-terminal alpha helices. The structure reveals KPHMT's membership in a small, recently discovered group of (beta/alpha) barrel enzymes that employ domain swapping to form a variety of oligomeric assemblies. The apparent conservation of certain detailed structural characteristics suggests that KPHMT is distantly related by divergent evolution to enzymes in unrelated pathways, including isocitrate lyase and phosphoenolpyruvate mutase. |
==About this Structure== | ==About this Structure== | ||
| - | 1OY0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_hydroxymethyltransferase 3-methyl-2-oxobutanoate hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.11 2.1.2.11] Full crystallographic information is available from [http:// | + | 1OY0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_hydroxymethyltransferase 3-methyl-2-oxobutanoate hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.11 2.1.2.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OY0 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chaudhuri, B | + | [[Category: Chaudhuri, B N.]] |
| - | [[Category: Kim, C | + | [[Category: Kim, C Y.]] |
| - | [[Category: Park, M | + | [[Category: Park, M S.]] |
| - | [[Category: Sawaya, M | + | [[Category: Sawaya, M R.]] |
| - | [[Category: TBSGC, TB | + | [[Category: TBSGC, TB Structural Genomics Consortium.]] |
| - | [[Category: Terwilliger, T | + | [[Category: Terwilliger, T C.]] |
| - | [[Category: Waldo, G | + | [[Category: Waldo, G S.]] |
| - | [[Category: Yeates, T | + | [[Category: Yeates, T O.]] |
[[Category: MG]] | [[Category: MG]] | ||
[[Category: domain swapping]] | [[Category: domain swapping]] | ||
| Line 30: | Line 30: | ||
[[Category: tbsgc]] | [[Category: tbsgc]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:23:01 2008'' |
Revision as of 12:23, 21 February 2008
|
The crystal Structure of the First Enzyme of Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase from Mycobacterium Tuberculosis Shows a Decameric Assembly and Terminal Helix-Swapping
Overview
Ketopantoate hydroxymethyltransferase (KPHMT) catalyzes the first committed step in the biosynthesis of pantothenate, which is a precursor to coenzyme A and is required for penicillin biosynthesis. The crystal structure of KPHMT from Mycobacterium tuberculosis was determined by the single anomalous substitution (SAS) method at 2.8 A resolution. KPHMT adopts a structure that is a variation on the (beta/alpha) barrel fold, with a metal binding site proximal to the presumed catalytic site. The protein forms a decameric complex, with subunits in opposing pentameric rings held together by a swapping of their C-terminal alpha helices. The structure reveals KPHMT's membership in a small, recently discovered group of (beta/alpha) barrel enzymes that employ domain swapping to form a variety of oligomeric assemblies. The apparent conservation of certain detailed structural characteristics suggests that KPHMT is distantly related by divergent evolution to enzymes in unrelated pathways, including isocitrate lyase and phosphoenolpyruvate mutase.
About this Structure
1OY0 is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. Active as 3-methyl-2-oxobutanoate hydroxymethyltransferase, with EC number 2.1.2.11 Full crystallographic information is available from OCA.
Reference
The crystal structure of the first enzyme in the pantothenate biosynthetic pathway, ketopantoate hydroxymethyltransferase, from M tuberculosis., Chaudhuri BN, Sawaya MR, Kim CY, Waldo GS, Park MS, Terwilliger TC, Yeates TO, Structure. 2003 Jul;11(7):753-64. PMID:12842039
Page seeded by OCA on Thu Feb 21 14:23:01 2008
Categories: 3-methyl-2-oxobutanoate hydroxymethyltransferase | Mycobacterium tuberculosis | Single protein | Chaudhuri, B N. | Kim, C Y. | Park, M S. | Sawaya, M R. | TBSGC, TB Structural Genomics Consortium. | Terwilliger, T C. | Waldo, G S. | Yeates, T O. | MG | Domain swapping | Protein structure initiative | Psi | Structural genomics | Tb structural genomics consortium | Tbsgc
