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| - | [[Image:1ig0.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ig0| PDB=1ig0 | SCENE= }} | | {{STRUCTURE_1ig0| PDB=1ig0 | SCENE= }} |
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| - | '''Crystal Structure of yeast Thiamin Pyrophosphokinase'''
| + | ===Crystal Structure of yeast Thiamin Pyrophosphokinase=== |
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| - | ==Overview==
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| - | BACKGROUND: Thiamin pyrophosphokinase (TPK) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the formation of a coenzyme required for central metabolic functions. TPK has no sequence homologs in the PDB and functions by an unknown mechanism. The TPK structure has been determined as a significant step toward elucidating its catalytic action. RESULTS: The crystal structure of Saccharomyces cerevisiae TPK complexed with thiamin has been determined at 1.8 A resolution. TPK is a homodimer, and each subunit consists of two domains. One domain resembles a Rossman fold with four alpha helices on each side of a 6 strand parallel beta sheet. The other domain has one 4 strand and one 6 strand antiparallel beta sheet, which form a flattened sandwich structure containing a jelly-roll topology. The active site is located in a cleft at the dimer interface and is formed from residues from domains of both subunits. The TPK dimer contains two compound active sites at the subunit interface. CONCLUSIONS: The structure of TPK with one substrate bound identifies the location of the thiamin binding site and probable catalytic residues. The structure also suggests a likely binding site for ATP. These findings are further supported by TPK sequence homologies. Although possessing no significant sequence homology with other pyrophospokinases, thiamin pyrophosphokinase may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11435118}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11435118 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11435118}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Compound active site]] | | [[Category: Compound active site]] |
| | [[Category: Protein-substrate complex]] | | [[Category: Protein-substrate complex]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:57:34 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:55:49 2008'' |
Revision as of 07:55, 1 July 2008
Template:STRUCTURE 1ig0
Crystal Structure of yeast Thiamin Pyrophosphokinase
Template:ABSTRACT PUBMED 11435118
About this Structure
1IG0 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The crystal structure of yeast thiamin pyrophosphokinase., Baker LJ, Dorocke JA, Harris RA, Timm DE, Structure. 2001 Jun;9(6):539-46. PMID:11435118
Page seeded by OCA on Tue Jul 1 10:55:49 2008
