1ggv

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(New page: 200px<br /><applet load="1ggv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ggv, resolution 2.50&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1ggv.gif|left|200px]]<br /><applet load="1ggv" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ggv, resolution 2.50&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE C123S MUTANT OF DIENELACTONE HYDROLASE (DLH) BOUND WITH THE PMS MOIETY OF THE PROTEASE INHIBITOR, PHENYLMETHYLSULFONYL FLUORIDE (PMSF)'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE C123S MUTANT OF DIENELACTONE HYDROLASE (DLH) BOUND WITH THE PMS MOIETY OF THE PROTEASE INHIBITOR, PHENYLMETHYLSULFONYL FLUORIDE (PMSF)==
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The structure of DLH (C123S) with PMS bound was solved to 2.5 A resolution, (R factor = 15.1%). PMSF in 2-propanol was delivered directly to crystals, in drops and unexpectedly caused the crystals to dissolve. New crystals, displaying a different morphology emerged within 2 h in situ, a phenomenon, that appears to be described for the first time. The changed crystal form, reflected altered crystal-packing arrangements elicited by structural, changes to the DLH (C123S) molecule on binding inhibitor. The new unit, cell remained in the P2(1)2(1)2(1) space group but possessed different, dimensions. The structure showed that PMS binding in DLH (C123S) caused, conformational changes in the active site and in four regions of the, polypeptide chain that contain reverse turns. In the active site, residues, with aromatic side chains were repositioned in an edge-to-face cluster, around the PMS phenyl ring. Their redistribution prevented restabilization, of the triad His202 side chain, which was disordered in electron-density, maps. Movements of other residues in the active site were shown to be, related to the four displaced regions of the polypeptide chain. Their, implied synergy suggests that DLH may be able to accommodate and catalyse, a range of compounds unrelated to the natural substrate owing to an, inherent coordinated flexibility in its overall structure. Implications, for mechanism and further engineering studies are discussed.
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<StructureSection load='1ggv' size='340' side='right'caption='[[1ggv]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1ggv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GGV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GGV FirstGlance]. <br>
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1GGV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Active as [http://en.wikipedia.org/wiki/Carboxymethylenebutenolidase Carboxymethylenebutenolidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.45 3.1.1.45] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GGV 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]] 2.5&#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=SEB:O-BENZYLSULFONYL-SERINE'>SEB</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=1ggv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ggv OCA], [https://pdbe.org/1ggv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ggv RCSB], [https://www.ebi.ac.uk/pdbsum/1ggv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ggv ProSAT]</span></td></tr>
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Structure of the C123S mutant of dienelactone hydrolase (DLH) bound with the PMS moiety of the protease inhibitor phenylmethylsulfonyl fluoride (PMSF)., Robinson A, Edwards KJ, Carr PD, Barton JD, Ewart GD, Ollis DL, Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1376-84. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11053834 11053834]
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</table>
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[[Category: Carboxymethylenebutenolidase]]
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== Function ==
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[https://www.uniprot.org/uniprot/CLCD_PSEPU CLCD_PSEPU] Ring cleavage of cyclic ester dienelactone to produce maleylacetate.
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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/gg/1ggv_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=1ggv 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: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
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[[Category: Single protein]]
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[[Category: Barton JD]]
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[[Category: Barton, J.D.]]
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[[Category: Carr PD]]
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[[Category: Carr, P.D.]]
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[[Category: Edwards KJ]]
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[[Category: Edwards, K.J.]]
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[[Category: Ewart GD]]
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[[Category: Ewart, G.D.]]
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[[Category: Ollis DL]]
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[[Category: Ollis, D.L.]]
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[[Category: Robinson A]]
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[[Category: Robinson, A.]]
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[[Category: alpha/beta hydrolase fold]]
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[[Category: dienelactone hydrolase]]
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[[Category: pmsf]]
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[[Category: pseudomonas putida (pac27)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:02:47 2007''
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Current revision

CRYSTAL STRUCTURE OF THE C123S MUTANT OF DIENELACTONE HYDROLASE (DLH) BOUND WITH THE PMS MOIETY OF THE PROTEASE INHIBITOR, PHENYLMETHYLSULFONYL FLUORIDE (PMSF)

PDB ID 1ggv

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