2pui
From Proteopedia
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| - | [[Image:2pui.gif|left|200px]] | + | [[Image:2pui.gif|left|200px]] |
| - | + | ||
| - | '''Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding''' | + | {{Structure |
| + | |PDB= 2pui |SIZE=350|CAPTION= <scene name='initialview01'>2pui</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= mtnK, ykrT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | }} | ||
| + | |||
| + | '''Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2PUI is a [ | + | 2PUI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PUI OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17522047 17522047] |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: S-methyl-5-thioribose kinase]] | [[Category: S-methyl-5-thioribose kinase]] | ||
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[[Category: methionine recycling pathway]] | [[Category: methionine recycling pathway]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:17:33 2008'' |
Revision as of 16:17, 20 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | mtnK, ykrT (Bacillus subtilis) | ||||||
| Activity: | S-methyl-5-thioribose kinase, with EC number 2.7.1.100 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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