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1p01

From Proteopedia

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(New page: 200px<br /><applet load="1p01" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p01, resolution 2.0&Aring;" /> '''SERINE PROTEASE MECHA...)
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[[Image:1p01.gif|left|200px]]<br /><applet load="1p01" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1p01, resolution 2.0&Aring;" />
 
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'''SERINE PROTEASE MECHANISM. STRUCTURE OF AN INHIBITORY COMPLEX OF ALPHA-LYTIC PROTEASE AND A TIGHTLY BOUND PEPTIDE BORONIC ACID'''<br />
 
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==Overview==
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==Serine protease mechanism. structure of an inhibitory complex oF ALPHA-LYTIC Protease and a tightly bound peptide boronic acid==
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The structure of the complex formed between alpha-lytic protease, a serine, protease secreted by Lysobacter enzymogenes, and, N-tert-butyloxycarbonylalanylprolylvaline boronic acid (Ki = 0.35 nM) has, been studied by X-ray crystallography to a resolution of 2.0 A. The, active-site serine forms a covalent, nearly tetrahedral adduct with the, boronic acid moiety of the inhibitor. The complex is stabilized by seven, hydrogen bonds between the enzyme and inhibitor with additional, stabilization arising from van der Waals interactions between enzyme and, inhibitor side chains and the burying of 330 A2 of hydrophobic surface, area. Hydrogen bonding between Asp-102 and His-57 remains intact in the, enzyme-inhibitor complex, and His N epsilon 2 is well positioned to donate, its hydrogen to the leaving group. Little change in the positions of, protease residues was observed on complex formation (root mean square main, chain deviation = 0.13 A), suggesting that in its native state the enzyme, is complementary to tetrahedral reaction intermediates or to the nearly, tetrahedral transition state for the reaction.
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<StructureSection load='1p01' size='340' side='right'caption='[[1p01]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1p01]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P01 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&#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=0EG:N-(TERT-BUTOXYCARBONYL)-L-ALANYL-N-[(1R)-1-(DIHYDROXYBORANYL)-2-METHYLPROPYL]-L-PROLINAMIDE'>0EG</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=1p01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p01 OCA], [https://pdbe.org/1p01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p01 RCSB], [https://www.ebi.ac.uk/pdbsum/1p01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p01 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/p0/1p01_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=1p01 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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1P01 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1P01 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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Serine protease mechanism: structure of an inhibitory complex of alpha-lytic protease and a tightly bound peptide boronic acid., Bone R, Shenvi AB, Kettner CA, Agard DA, Biochemistry. 1987 Dec 1;26(24):7609-14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=3122831 3122831]
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[[Category: Large Structures]]
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[[Category: Alpha-lytic endopeptidase]]
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[[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: Bone R]]
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[[Category: Bone, R.]]
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[[Category: SO4]]
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[[Category: hydrolase (serine proteinase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:19:57 2007''
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Current revision

Serine protease mechanism. structure of an inhibitory complex oF ALPHA-LYTIC Protease and a tightly bound peptide boronic acid

PDB ID 1p01

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