1ig3: Difference between revisions
New page: left|200px<br /><applet load="1ig3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ig3, resolution 1.90Å" /> '''Mouse Thiamin Pyroph... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1ig3.gif|left|200px]]<br /><applet load="1ig3" size=" | [[Image:1ig3.gif|left|200px]]<br /><applet load="1ig3" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ig3, resolution 1.90Å" /> | caption="1ig3, resolution 1.90Å" /> | ||
'''Mouse Thiamin Pyrophosphokinase Complexed with Thiamin'''<br /> | '''Mouse Thiamin Pyrophosphokinase Complexed with Thiamin'''<br /> | ||
==Overview== | ==Overview== | ||
Thiamin pyrophosphate (TPP) is a coenzyme derived from vitamin B1 | Thiamin pyrophosphate (TPP) is a coenzyme derived from vitamin B1 (thiamin). TPP synthesis in eukaryotes requires thiamin pyrophosphokinase (TPK), which catalyzes the transfer of a pyrophosphate group from ATP to thiamin. TPP is essential for central metabolic processes, including the formation of acetyl CoA from glucose and the Krebs cycle. Deficiencies in human thiamin metabolism result in beriberi and Wernicke encephalopathy. The crystal structure of mouse TPK was determined by multiwavelength anomalous diffraction at 2.4 A resolution, and the structure of TPK complexed with thiamin has been refined at 1.9 A resolution. The TPK polypeptide folds as an alpha/beta-domain and a beta-sandwich domain, which share a central ten-stranded mixed beta-sheet. TPK subunits associate as a dimer, and thiamin is bound in the dimer interface. Despite lacking apparent sequence homology with other proteins, the alpha/beta-domain resembles the Rossman fold and is similar to other kinase structures, including another pyrophosphokinase and a thiamin biosynthetic enzyme. Comparison of mouse and yeast TPK structures reveals differences that could be exploited in developing species-specific inhibitors of potential use as antimicrobial agents. | ||
==About this Structure== | ==About this Structure== | ||
1IG3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4 and VIB as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thiamine_diphosphokinase Thiamine diphosphokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.6.2 2.7.6.2] Full crystallographic information is available from [http:// | 1IG3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=VIB:'>VIB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thiamine_diphosphokinase Thiamine diphosphokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.6.2 2.7.6.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IG3 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thiamine diphosphokinase]] | [[Category: Thiamine diphosphokinase]] | ||
[[Category: Baker, L | [[Category: Baker, L J.]] | ||
[[Category: Harris, R | [[Category: Harris, R A.]] | ||
[[Category: Liu, J.]] | [[Category: Liu, J.]] | ||
[[Category: Timm, D | [[Category: Timm, D E.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: VIB]] | [[Category: VIB]] | ||
| Line 23: | Line 23: | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:33 2008'' | ||
Revision as of 14:11, 21 February 2008
|
Mouse Thiamin Pyrophosphokinase Complexed with Thiamin
OverviewOverview
Thiamin pyrophosphate (TPP) is a coenzyme derived from vitamin B1 (thiamin). TPP synthesis in eukaryotes requires thiamin pyrophosphokinase (TPK), which catalyzes the transfer of a pyrophosphate group from ATP to thiamin. TPP is essential for central metabolic processes, including the formation of acetyl CoA from glucose and the Krebs cycle. Deficiencies in human thiamin metabolism result in beriberi and Wernicke encephalopathy. The crystal structure of mouse TPK was determined by multiwavelength anomalous diffraction at 2.4 A resolution, and the structure of TPK complexed with thiamin has been refined at 1.9 A resolution. The TPK polypeptide folds as an alpha/beta-domain and a beta-sandwich domain, which share a central ten-stranded mixed beta-sheet. TPK subunits associate as a dimer, and thiamin is bound in the dimer interface. Despite lacking apparent sequence homology with other proteins, the alpha/beta-domain resembles the Rossman fold and is similar to other kinase structures, including another pyrophosphokinase and a thiamin biosynthetic enzyme. Comparison of mouse and yeast TPK structures reveals differences that could be exploited in developing species-specific inhibitors of potential use as antimicrobial agents.
About this StructureAbout this Structure
1IG3 is a Single protein structure of sequence from Mus musculus with and as ligands. Active as Thiamine diphosphokinase, with EC number 2.7.6.2 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of thiamin pyrophosphokinase., Timm DE, Liu J, Baker LJ, Harris RA, J Mol Biol. 2001 Jun 29;310(1):195-204. PMID:11419946
Page seeded by OCA on Thu Feb 21 13:11:33 2008