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1gbk

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(New page: 200px<br /><applet load="1gbk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gbk, resolution 2.13&Aring;" /> '''ALPHA-LYTIC PROTEASE...)
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[[Image:1gbk.gif|left|200px]]<br /><applet load="1gbk" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gbk, resolution 2.13&Aring;" />
 
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'''ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID'''<br />
 
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==Overview==
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==ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID==
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Gly216 in the active site of the broadly specific MA190 mutant of, alpha-lytic protease has been found to be remarkably tolerant of amino, acid substitutions. Side-chains as large as Trp can be accommodated within, the substrate-binding pocket without abolishing catalysis, and have major, effects upon the substrate specificity of the enzyme. Kinetic, characterization of eleven enzymatically active mutants against a panel of, eight substrates clearly revealed the functional consequences of the, substitutions at position 216. To understand better the structural basis, for their altered specificity, the GA216 + MA190 and GL216 + MA190 mutants, have been crystallized both with and without a representative series of, peptide boronic acid transition-state analog inhibitors. An empirical, description and non-parametric statistical analysis of structural, variation among these enzyme: inhibitor complexes is presented. The roles, of active site plasticity and dynamics in alpha-lytic protease function, and substrate preference are also addressed. The results strongly suggest, that substrate specificity determination in alpha-lytic protease is a, distributed property of the active site and substrate molecule.
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<StructureSection load='1gbk' size='340' side='right'caption='[[1gbk]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1gbk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1lpr 1lpr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GBK FirstGlance]. <br>
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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]] 2.13&#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=B2A:ALANINE+BORONIC+ACID'>B2A</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=1gbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gbk OCA], [https://pdbe.org/1gbk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gbk RCSB], [https://www.ebi.ac.uk/pdbsum/1gbk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gbk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PRLA_LYSEN PRLA_LYSEN]
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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/gb/1gbk_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=1gbk ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1GBK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1LPR. Active as [http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GBK OCA].
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*[[Alpha-lytic protease 3D structures|Alpha-lytic protease 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity., Mace JE, Agard DA, J Mol Biol. 1995 Dec 8;254(4):720-36. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7500345 7500345]
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[[Category: Large Structures]]
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[[Category: Alpha-lytic endopeptidase]]
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[[Category: Lysobacter enzymogenes]]
[[Category: Lysobacter enzymogenes]]
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[[Category: Single protein]]
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[[Category: Agard DA]]
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[[Category: Agard, D.A.]]
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[[Category: Mace JE]]
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[[Category: Mace, J.E.]]
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[[Category: SO4]]
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[[Category: active-site mutation]]
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[[Category: inhibitor complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:54:34 2007''
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Current revision

ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID

PDB ID 1gbk

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