2pui
From Proteopedia
(New page: 200px<br /><applet load="2pui" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pui, resolution 2.20Å" /> '''Structures of 5-meth...) |
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| - | [[Image:2pui.gif|left|200px]]<br /><applet load="2pui" size=" | + | [[Image:2pui.gif|left|200px]]<br /><applet load="2pui" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2pui, resolution 2.20Å" /> | caption="2pui, resolution 2.20Å" /> | ||
'''Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding'''<br /> | '''Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2PUI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with MG, CPS and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/S-methyl-5-thioribose_kinase S-methyl-5-thioribose kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.100 2.7.1.100] Full crystallographic information is available from [http:// | + | 2PUI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CPS:'>CPS</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/S-methyl-5-thioribose_kinase S-methyl-5-thioribose kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.100 2.7.1.100] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PUI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: methionine recycling pathway]] | [[Category: methionine recycling pathway]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:14:41 2008'' |
Revision as of 12:14, 23 January 2008
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Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding
Overview
The methionine salvage pathway is ubiquitous in all organisms, but, metabolic variations exist between bacteria and mammals., 5-Methylthioribose (MTR) kinase is a key enzyme in methionine salvage in, bacteria and the absence of a mammalian homolog suggests that it is a good, target for the design of novel antibiotics. The structures of the apo-form, of Bacillus subtilis MTR kinase, as well as its ADP, ADP-PO(4), AMPPCP, and AMPPCP-MTR complexes have been determined. MTR kinase has a bilobal, eukaryotic protein kinase fold but exhibits a number of unique features., The protein lacks the DFG motif typically found at the beginning of the, activation loop and instead coordinates magnesium via a DXE motif, (Asp(250)-Glu(252)). In addition, the glycine-rich loop of the protein, analogous to the "Gly triad" in protein kinases, does not interact, extensively with the nucleotide. The MTR substrate-binding site consists, of Asp(233) of the catalytic HGD motif, a novel twin arginine motif, (Arg(340)/Arg(341)), and a semi-conserved W-loop, which appears to, regulate MTR binding specificity. No lobe closure is observed for MTR, kinase upon substrate binding. This is probably because the enzyme lacks, the lobe closure/inducing interactions between the C-lobe of the protein, and the ribosyl moiety of the nucleotide that are typically responsible, for lobe closure in protein kinases. The current structures suggest that, MTR kinase has a dissociative mechanism.
About this Structure
2PUI is a Single protein structure of sequence from Bacillus subtilis with , and as ligands. Active as S-methyl-5-thioribose kinase, with EC number 2.7.1.100 Full crystallographic information is available from OCA.
Reference
Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding., Ku SY, Yip P, Cornell KA, Riscoe MK, Behr JB, Guillerm G, Howell PL, J Biol Chem. 2007 Jul 27;282(30):22195-206. Epub 2007 May 23. PMID:17522047
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