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2pui

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[[Image:2pui.gif|left|200px]]
 
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{{Structure
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==Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding==
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|PDB= 2pui |SIZE=350|CAPTION= <scene name='initialview01'>2pui</scene>, resolution 2.20&Aring;
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<StructureSection load='2pui' size='340' side='right'caption='[[2pui]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|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>
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<table><tr><td colspan='2'>[[2pui]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PUI FirstGlance]. <br>
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|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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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|GENE= mtnK, ykrT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pui OCA], [https://pdbe.org/2pui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pui RCSB], [https://www.ebi.ac.uk/pdbsum/2pui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pui ProSAT]</span></td></tr>
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</table>
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'''Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding'''
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== Function ==
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[https://www.uniprot.org/uniprot/MTNK_BACSU MTNK_BACSU] Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate.<ref>PMID:11545674</ref>
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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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.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pu/2pui_consurf.spt"</scriptWhenChecked>
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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].
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==Reference==
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</jmolCheckbox>
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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]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2pui ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: S-methyl-5-thioribose kinase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Ku S-Y]]
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[[Category: Ku, S Y.]]
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[[Category: ADP]]
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[[Category: CPS]]
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[[Category: MG]]
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[[Category: 5-methylthioribose kinase]]
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[[Category: methionine recycling pathway]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:17:33 2008''
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Current revision

Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding

PDB ID 2pui

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