1fwk

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(New page: 200px<br /><applet load="1fwk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fwk, resolution 2.1&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1fwk.jpg|left|200px]]<br /><applet load="1fwk" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fwk, resolution 2.1&Aring;" />
 
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'''CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ADP'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ADP==
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BACKGROUND: Homoserine kinase (HSK) catalyzes an important step in the, threonine biosynthesis pathway. It belongs to a large yet unique class of, small metabolite kinases, the GHMP kinase superfamily. Members in the GHMP, superfamily participate in several essential metabolic pathways, such as, amino acid biosynthesis, galactose metabolism, and the mevalonate pathway., RESULTS: The crystal structure of HSK and its complex with ADP reveal a, novel nucleotide binding fold. The N-terminal domain contains an unusual, left-handed betaalphabeta unit, while the C-terminal domain has a central, alpha-beta plait fold with an insertion of four helices. The phosphate, binding loop in HSK is distinct from the classical P loops found in many, ATP/GTP binding proteins. The bound ADP molecule adopts a rare syn, conformation and is in the opposite orientation from those bound to the P, loop-containing proteins. Inspection of the substrate binding cavity, indicates several amino acid residues that are likely to be involved in, substrate binding and catalysis. CONCLUSIONS: The crystal structure of HSK, is the first representative in the GHMP superfamily to have determined, structure. It provides insight into the structure and nucleotide binding, mechanism of not only the HSK family but also a variety of enzymes in the, GHMP superfamily. Such enzymes include galactokinases, mevalonate kinases, phosphomevalonate kinases, mevalonate pyrophosphate decarboxylases, and, several proteins of yet unknown functions.
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<StructureSection load='1fwk' size='340' side='right'caption='[[1fwk]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1fwk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FWK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FWK FirstGlance]. <br>
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1FWK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Homoserine_kinase Homoserine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.39 2.7.1.39] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FWK OCA].
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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]] 2.1&#8491;</td></tr>
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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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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==Reference==
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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=1fwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fwk OCA], [https://pdbe.org/1fwk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fwk RCSB], [https://www.ebi.ac.uk/pdbsum/1fwk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fwk ProSAT]</span></td></tr>
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Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily., Zhou T, Daugherty M, Grishin NV, Osterman AL, Zhang H, Structure. 2000 Dec 15;8(12):1247-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11188689 11188689]
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</table>
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[[Category: Homoserine kinase]]
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== Function ==
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[https://www.uniprot.org/uniprot/KHSE_METJA KHSE_METJA] Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fw/1fwk_consurf.spt"</scriptWhenChecked>
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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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</jmolCheckbox>
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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=1fwk ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Methanocaldococcus jannaschii]]
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[[Category: Single protein]]
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[[Category: Daugherty M]]
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[[Category: Daugherty, M.]]
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[[Category: Grishin NV]]
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[[Category: Grishin, N.V.]]
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[[Category: Osterman AL]]
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[[Category: Osterman, A.L.]]
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[[Category: Zhang H]]
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[[Category: Zhang, H.]]
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[[Category: Zhou T]]
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[[Category: Zhou, T.]]
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[[Category: ADP]]
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[[Category: MG]]
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[[Category: kinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:22:44 2007''
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Current revision

CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ADP

PDB ID 1fwk

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