1p01

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{{Seed}}
 
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[[Image:1p01.png|left|200px]]
 
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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 line below this paragraph, containing "STRUCTURE_1p01", creates the "Structure Box" on the page.
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<StructureSection load='1p01' size='340' side='right'caption='[[1p01]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_1p01| PDB=1p01 | SCENE= }}
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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/initialview03.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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===SERINE PROTEASE MECHANISM. STRUCTURE OF AN INHIBITORY COMPLEX OF ALPHA-LYTIC PROTEASE AND A TIGHTLY BOUND PEPTIDE BORONIC ACID===
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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:3122831<ref>PMID:3122831</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1p01" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_3122831}}, adds the Publication Abstract to the page
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*[[Alpha-lytic protease 3D structures|Alpha-lytic protease 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 3122831 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_3122831}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1P01 is a 2 chains structure of sequences from [http://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].
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==Reference==
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<ref group="xtra">PMID:3122831</ref><references group="xtra"/>
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[[Category: Alpha-lytic endopeptidase]]
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[[Category: Lysobacter enzymogenes]]
[[Category: Lysobacter enzymogenes]]
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[[Category: Agard, D A.]]
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[[Category: Agard DA]]
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[[Category: Bone, R.]]
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[[Category: Bone R]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Sep 21 19:50:05 2009''
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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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