1p05 - Revision history

OCA at 05:52, 17 April 2024

OCA — Wed, 17 Apr 2024 05:52:07 GMT

←Older revision		Revision as of 05:52, 17 April 2024
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	<StructureSection load='1p05' size='340' side='right'caption='[[1p05]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1p05' size='340' side='right'caption='[[1p05]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1p05]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_29487 Atcc 29487~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P05 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1p05]] is a 2 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=1P05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P05 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.1Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNO:NORLEUCINE+BORONIC+ACID'>BNO</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BNO:NORLEUCINE+BORONIC+ACID'>BNO</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12]~~ </~~span~~></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p05 OCA], [https://pdbe.org/1p05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p05 RCSB], [https://www.ebi.ac.uk/pdbsum/1p05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p05 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p05 OCA], [https://pdbe.org/1p05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p05 RCSB], [https://www.ebi.ac.uk/pdbsum/1p05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p05 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/PRLA_LYSEN PRLA_LYSEN]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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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=1p05 ConSurf].		</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=1p05 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	To better understand the structural basis of enzyme specificity, the structures of complexes formed between alpha-lytic protease, an extracellular serine protease of Lysobacter enzymogenes, and five inhibitory peptide boronic acids (R2-boroX, where R2 is methoxysuccinyl-Ala-Ala-Pro- and boroX is the alpha-aminoboronic acid analogue of Ala, Val, Ile, Norleu, or Phe) have been studied at high resolution by X-ray crystallography. The enzyme has primary specificity for Ala in the P1 position of peptide substrates with catalytic efficiency decreasing with increasing side-chain volume. Enzyme affinity for inhibitors with boroVal, boroIle, and boroPhe residues is much higher than expected on the basis of the catalytic efficiencies of homologous substrates. Covalent tetrahedral adducts are formed between the active-site serine and the boronic acid moieties of R2-boroAla, R2-boroVal R2-boroIle, and R2-boroNorleu. Though R2-boroVal is a slowly bound inhibitor and R2-boroAla is rapidly bound [Kettner, C. A., Bone, R., Agard, D. A., & Bachovchin, W. W. (1988) Biochemistry 27, 7682-7688], there appear to be no structural differences that could account for slow binding. The removal from solution of 20% more hydrophobic surface on binding accounts for the improved affinity of alpha-lytic protease for R2-boroVal relative to R2-boroAla. The high affinity of the enzyme for R2-boroIle derives from the selective binding of the L-allo stereoisomer of the boroIle residue, which can avoid bad steric interactions in the binding pocket.(ABSTRACT TRUNCATED AT 250 WORDS)
-
-	Structural analysis of specificity: alpha-lytic protease complexes with analogues of reaction intermediates.,Bone R, Frank D, Kettner CA, Agard DA Biochemistry. 1989 Sep 19;28(19):7600-9. PMID:2611204<ref>PMID:2611204</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1p05" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Alpha-lytic protease 3D structures\|Alpha-lytic protease 3D structures]]		*[[Alpha-lytic protease 3D structures\|Alpha-lytic protease 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Alpha-lytic endopeptidase]]
-	[[Category: Atcc 29487]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Agard, D A~~]]	+	[[Category: Lysobacter enzymogenes]]
-	[[Category: ~~Bone, R~~]]	+	[[Category: Agard DA]]
-	[[Category: ~~Hydrolase-hydrolase inhibitor complex~~]]	+	[[Category: Bone R]]

OCA at 09:23, 8 September 2021

OCA — Wed, 08 Sep 2021 09:23:19 GMT

←Older revision		Revision as of 09:23, 8 September 2021
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	<StructureSection load='1p05' size='340' side='right'caption='[[1p05]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1p05' size='340' side='right'caption='[[1p05]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1p05]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_29487 Atcc 29487]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P05 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1P05 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1p05]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_29487 Atcc 29487]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P05 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNO:NORLEUCINE+BORONIC+ACID'>BNO</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNO:NORLEUCINE+BORONIC+ACID'>BNO</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~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] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1p05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p05 OCA], [~~http~~://pdbe.org/1p05 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1p05 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1p05 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1p05 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p05 OCA], [https://pdbe.org/1p05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p05 RCSB], [https://www.ebi.ac.uk/pdbsum/1p05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p05 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 10:21, 27 November 2019

OCA — Wed, 27 Nov 2019 10:21:56 GMT

←Older revision		Revision as of 10:21, 27 November 2019
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	==STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES==		==STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES==
-	<StructureSection load='1p05' size='340' side='right' caption='[[1p05]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='1p05' size='340' side='right'caption='[[1p05]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1p05]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29487 Atcc 29487]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P05 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1p05]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29487 Atcc 29487]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P05 FirstGlance]. <br>
Line 30:		Line 30:

	==See Also==		==See Also==
-	*[[Alpha-lytic protease\|Alpha-lytic protease]]	+	*[[Alpha-lytic protease 3D structures\|Alpha-lytic protease 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 37:
	[[Category: Alpha-lytic endopeptidase]]		[[Category: Alpha-lytic endopeptidase]]
	[[Category: Atcc 29487]]		[[Category: Atcc 29487]]
		+	[[Category: Large Structures]]
	[[Category: Agard, D A]]		[[Category: Agard, D A]]
	[[Category: Bone, R]]		[[Category: Bone, R]]
	[[Category: Hydrolase-hydrolase inhibitor complex]]		[[Category: Hydrolase-hydrolase inhibitor complex]]

OCA at 07:51, 15 February 2018

OCA — Thu, 15 Feb 2018 07:51:00 GMT

←Older revision		Revision as of 07:51, 15 February 2018
Line 1:		Line 1:
		+
	==STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES==		==STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES==
	<StructureSection load='1p05' size='340' side='right' caption='[[1p05]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1p05' size='340' side='right' caption='[[1p05]], [[Resolution\|resolution]] 2.10Å' scene=''>
Line 6:		Line 7:
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNO:NORLEUCINE+BORONIC+ACID'>BNO</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNO:NORLEUCINE+BORONIC+ACID'>BNO</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p05 OCA], [http://pdbe.org/1p05 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p05 RCSB], [http://www.ebi.ac.uk/pdbsum/1p05 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p05 OCA], [http://pdbe.org/1p05 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p05 RCSB], [http://www.ebi.ac.uk/pdbsum/1p05 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p05 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p0/1p05_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p0/1p05_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 03:14, 7 February 2016

OCA — Sun, 07 Feb 2016 03:14:27 GMT

←Older revision		Revision as of 03:14, 7 February 2016
Line 16:		Line 16:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</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/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</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=1p05 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 21:07, 9 September 2015

OCA — Wed, 09 Sep 2015 21:07:58 GMT

←Older revision		Revision as of 21:07, 9 September 2015
Line 2:		Line 2:
	<StructureSection load='1p05' size='340' side='right' caption='[[1p05]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1p05' size='340' side='right' caption='[[1p05]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1p05]] is a 2 chain structure with sequence 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=1P05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P05 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1p05]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29487 Atcc 29487]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P05 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNO:NORLEUCINE+BORONIC+ACID'>BNO</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNO:NORLEUCINE+BORONIC+ACID'>BNO</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p05 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p05 RCSB], [http://www.ebi.ac.uk/pdbsum/1p05 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p05 OCA], [http://pdbe.org/1p05 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p05 RCSB], [http://www.ebi.ac.uk/pdbsum/1p05 PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 26:		Line 26:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1p05" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Alpha-lytic endopeptidase]]		[[Category: Alpha-lytic endopeptidase]]
-	[[Category: ~~Lysobacter enzymogenes~~]]	+	[[Category: Atcc 29487]]
	[[Category: Agard, D A]]		[[Category: Agard, D A]]
	[[Category: Bone, R]]		[[Category: Bone, R]]
	[[Category: Hydrolase-hydrolase inhibitor complex]]		[[Category: Hydrolase-hydrolase inhibitor complex]]

OCA at 07:20, 6 January 2015

OCA — Tue, 06 Jan 2015 07:20:11 GMT

←Older revision		Revision as of 07:20, 6 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1p05]] is a 2 chain structure with sequence 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=1P05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P05 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1p05]] is a 2 chain structure with sequence 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=1P05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P05 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNO:NORLEUCINE+BORONIC+ACID'>BNO</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNO:NORLEUCINE+BORONIC+ACID'>BNO</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p05 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p05 RCSB], [http://www.ebi.ac.uk/pdbsum/1p05 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p05 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p05 RCSB], [http://www.ebi.ac.uk/pdbsum/1p05 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 35:
	[[Category: Alpha-lytic endopeptidase]]		[[Category: Alpha-lytic endopeptidase]]
	[[Category: Lysobacter enzymogenes]]		[[Category: Lysobacter enzymogenes]]
-	[[Category: Agard, D A.]]	+	[[Category: Agard, D A]]
-	[[Category: Bone, R.]]	+	[[Category: Bone, R]]
	[[Category: Hydrolase-hydrolase inhibitor complex]]		[[Category: Hydrolase-hydrolase inhibitor complex]]

OCA at 19:47, 28 September 2014

OCA — Sun, 28 Sep 2014 19:47:10 GMT

←Older revision		Revision as of 19:47, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1p05.~~png~~\|~~left~~\|200px]]	+	==STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES==
		+	<StructureSection load='1p05' size='340' side='right' caption='[[1p05]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1p05]] is a 2 chain structure with sequence 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=1P05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P05 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNO:NORLEUCINE+BORONIC+ACID'>BNO</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p05 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p05 RCSB], [http://www.ebi.ac.uk/pdbsum/1p05 PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p0/1p05_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</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/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	To better understand the structural basis of enzyme specificity, the structures of complexes formed between alpha-lytic protease, an extracellular serine protease of Lysobacter enzymogenes, and five inhibitory peptide boronic acids (R2-boroX, where R2 is methoxysuccinyl-Ala-Ala-Pro- and boroX is the alpha-aminoboronic acid analogue of Ala, Val, Ile, Norleu, or Phe) have been studied at high resolution by X-ray crystallography. The enzyme has primary specificity for Ala in the P1 position of peptide substrates with catalytic efficiency decreasing with increasing side-chain volume. Enzyme affinity for inhibitors with boroVal, boroIle, and boroPhe residues is much higher than expected on the basis of the catalytic efficiencies of homologous substrates. Covalent tetrahedral adducts are formed between the active-site serine and the boronic acid moieties of R2-boroAla, R2-boroVal R2-boroIle, and R2-boroNorleu. Though R2-boroVal is a slowly bound inhibitor and R2-boroAla is rapidly bound [Kettner, C. A., Bone, R., Agard, D. A., & Bachovchin, W. W. (1988) Biochemistry 27, 7682-7688], there appear to be no structural differences that could account for slow binding. The removal from solution of 20% more hydrophobic surface on binding accounts for the improved affinity of alpha-lytic protease for R2-boroVal relative to R2-boroAla. The high affinity of the enzyme for R2-boroIle derives from the selective binding of the L-allo stereoisomer of the boroIle residue, which can avoid bad steric interactions in the binding pocket.(ABSTRACT TRUNCATED AT 250 WORDS)

-	~~{{STRUCTURE_1p05\| PDB=1p05 \| SCENE= }}~~	+	Structural analysis of specificity: alpha-lytic protease complexes with analogues of reaction intermediates.,Bone R, Frank D, Kettner CA, Agard DA Biochemistry. 1989 Sep 19;28(19):7600-9. PMID:2611204<ref>PMID:2611204</ref>

-	~~===STRUCTURE ANALYSIS OF SPECIFICITY~~. ~~ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_2611204}}~~	+	==See Also==
-		+	*[[Alpha-lytic protease\|Alpha-lytic protease]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1p05~~]] is a 2 chain structure with sequence 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=1P05 OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:002611204<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Alpha-lytic endopeptidase]]		[[Category: Alpha-lytic endopeptidase]]
	[[Category: Lysobacter enzymogenes]]		[[Category: Lysobacter enzymogenes]]

OCA: Protected "1p05" [edit=sysop:move=sysop]

OCA — Wed, 12 Dec 2012 21:52:33 GMT

Protected "1p05" [edit=sysop:move=sysop]

←Older revision

Revision as of 21:52, 12 December 2012

OCA at 21:52, 12 December 2012

OCA — Wed, 12 Dec 2012 21:52:27 GMT

←Older revision		Revision as of 21:52, 12 December 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1p05.png\|left\|200px]]		[[Image:1p05.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1p05", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
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	{{STRUCTURE_1p05\| PDB=1p05 \| SCENE= }}		{{STRUCTURE_1p05\| PDB=1p05 \| SCENE= }}

	===STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES===		===STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_2611204}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 2611204 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_2611204}}		{{ABSTRACT_PUBMED_2611204}}

	==About this Structure==		==About this Structure==
-	~~1P05~~ 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=1P05 OCA].	+	[[1p05]] is a 2 chain structure with sequence 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=1P05 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~2611204~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:002611204</ref><references group="xtra"/>
	[[Category: Alpha-lytic endopeptidase]]		[[Category: Alpha-lytic endopeptidase]]
	[[Category: Lysobacter enzymogenes]]		[[Category: Lysobacter enzymogenes]]
	[[Category: Agard, D A.]]		[[Category: Agard, D A.]]
	[[Category: Bone, R.]]		[[Category: Bone, R.]]
-		+	[[Category: Hydrolase-hydrolase inhibitor complex]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Mon Sep 21 19:50:21 2009''~~	+