4q4e - Revision history

OCA at 19:24, 29 May 2024

2024-05-29T19:24:33Z

←Older revision		Revision as of 19:24, 29 May 2024
Line 1:		Line 1:

	==Crystal structure of E.coli aminopeptidase N in complex with actinonin==		==Crystal structure of E.coli aminopeptidase N in complex with actinonin==
-	<StructureSection load='4q4e' size='340' side='right'caption='[[4q4e]]' scene=''>	+	<StructureSection load='4q4e' size='340' side='right'caption='[[4q4e]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q4E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4q4e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q4E FirstGlance]. <br>
-	</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=4q4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4e OCA], [https://pdbe.org/4q4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q4e RCSB], [https://www.ebi.ac.uk/pdbsum/4q4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q4e ProSAT]</span></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]] 1.9Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BB2:ACTINONIN'>BB2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4q4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4e OCA], [https://pdbe.org/4q4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q4e RCSB], [https://www.ebi.ac.uk/pdbsum/4q4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q4e ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/AMPN_ECOLI AMPN_ECOLI] Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Actinonin is a pseudotripeptide that displays a high affinity towards metalloproteases including peptide deformylases (PDFs) and M1 family aminopeptidases. PDF and M1 family aminopeptidases belong to thermolysin-metzincin superfamily. One of the major differences in terms of substrate binding pockets between these families is presence (in M1 aminopeptidases) or absence (in PDFs) of an S1 substrate pocket. The binding mode of actinonin to PDFs has been established previously; however, it is not clear how the actinonin, without a P1 residue, would bind to the M1 aminopeptidases. Here we describe the crystal structure of Escherichia coli aminopeptidase N (ePepN), a model protein of the M1 family aminopeptidases in complex with actinonin. For comparison we have also determined the structure of ePepN in complex with a well-known tetrapeptide inhibitor, amastatin. From the comparison of the actinonin and amastatin ePepN complexes, it is clear that the P1 residue is not critical as long as strong metal chelating head groups, like hydroxamic acid or alpha-hydroxy ketone, are present. Results from this study will be useful for the design of selective and efficient hydroxamate inhibitors against M1 family aminopeptidases.
		+
		+	Structural basis for the inhibition of M1 family aminopeptidases by the natural product actinonin: Crystal structure in complex with E. coli aminopeptidase N.,Ganji RJ, Reddi R, Gumpena R, Marapaka AK, Arya T, Sankoju P, Bhukya S, Addlagatta A Protein Sci. 2015 Feb 2. doi: 10.1002/pro.2653. PMID:25644575<ref>PMID:25644575</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4q4e" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]		*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Escherichia coli K-12]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Addlagatta A]]		[[Category: Addlagatta A]]
	[[Category: Ganji RJ]]		[[Category: Ganji RJ]]
	[[Category: Reddi R]]		[[Category: Reddi R]]

OCA at 10:54, 31 August 2022

2022-08-31T10:54:11Z

←Older revision		Revision as of 10:54, 31 August 2022
Line 1:		Line 1:

	==Crystal structure of E.coli aminopeptidase N in complex with actinonin==		==Crystal structure of E.coli aminopeptidase N in complex with actinonin==
-	<StructureSection load='4q4e' size='340' side='right'caption='[[4q4e]]~~, [[Resolution\|resolution]] 1.90Å~~' scene=''>	+	<StructureSection load='4q4e' size='340' side='right'caption='[[4q4e]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[4q4e]] is a 1 chain structure.~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q4E FirstGlance]. <br>	+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q4E FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BB2:ACTINONIN'>BB2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</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=4q4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4e OCA], [https://pdbe.org/4q4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q4e RCSB], [https://www.ebi.ac.uk/pdbsum/4q4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q4e ProSAT]</span></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4q4i\|4q4i]]</div></td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] </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=4q4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4e OCA], [https://pdbe.org/4q4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q4e RCSB], [https://www.ebi.ac.uk/pdbsum/4q4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q4e ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Function ==
-	[[https://www.uniprot.org/uniprot/AMPN_ECOLI AMPN_ECOLI]] Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Actinonin is a pseudotripeptide that displays a high affinity towards metalloproteases including peptide deformylases (PDFs) and M1 family aminopeptidases. PDF and M1 family aminopeptidases belong to thermolysin-metzincin superfamily. One of the major differences in terms of substrate binding pockets between these families is presence (in M1 aminopeptidases) or absence (in PDFs) of an S1 substrate pocket. The binding mode of actinonin to PDFs has been established previously; however, it is not clear how the actinonin, without a P1 residue, would bind to the M1 aminopeptidases. Here we describe the crystal structure of Escherichia coli aminopeptidase N (ePepN), a model protein of the M1 family aminopeptidases in complex with actinonin. For comparison we have also determined the structure of ePepN in complex with a well-known tetrapeptide inhibitor, amastatin. From the comparison of the actinonin and amastatin ePepN complexes, it is clear that the P1 residue is not critical as long as strong metal chelating head groups, like hydroxamic acid or alpha-hydroxy ketone, are present. Results from this study will be useful for the design of selective and efficient hydroxamate inhibitors against M1 family aminopeptidases.
-
-	Structural basis for the inhibition of M1 family aminopeptidases by the natural product actinonin: Crystal structure in complex with E. coli aminopeptidase N.,Ganji RJ, Reddi R, Gumpena R, Marapaka AK, Arya T, Sankoju P, Bhukya S, Addlagatta A Protein Sci. 2015 Feb 2. doi: 10.1002/pro.2653. PMID:25644575<ref>PMID:25644575</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4q4e" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]		*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Membrane alanyl aminopeptidase]]~~	+	[[Category: Addlagatta A]]
-	[[Category: Addlagatta, A]]	+	[[Category: Ganji RJ]]
-	[[Category: Ganji~~, R J~~]]	+	[[Category: Reddi R]]
-	[[Category: Reddi, R]]	+
-	~~[[Category: Aminopeptidase]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 05:06, 25 August 2022

2022-08-25T05:06:43Z

←Older revision		Revision as of 05:06, 25 August 2022
Line 3:		Line 3:
	<StructureSection load='4q4e' size='340' side='right'caption='[[4q4e]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='4q4e' size='340' side='right'caption='[[4q4e]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4q4e]] is a 1 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4E OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4Q4E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4q4e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q4E FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BB2:ACTINONIN'>BB2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BB2:ACTINONIN'>BB2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">~~[[4q4i\|4q4i]]~~<~~/td></tr>~~	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4q4i\|4q4i]]</div></td></tr>
-	~~<tr id~~='~~gene~~'~~><td class="sblockLbl"><b~~>[[~~Gene~~\|~~Gene:~~]]</b>~~</td><td class="sblockDat">pepN, b0932, JW0915 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])~~</td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] </span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] </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=4q4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4e OCA], [https://pdbe.org/4q4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q4e RCSB], [https://www.ebi.ac.uk/pdbsum/4q4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q4e ProSAT]</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=4q4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4e OCA], [~~http~~://pdbe.org/4q4e PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4q4e RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4q4e PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4q4e ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/AMPN_ECOLI AMPN_ECOLI]] Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation.	+	[[https://www.uniprot.org/uniprot/AMPN_ECOLI AMPN_ECOLI]] Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 28:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Ecoli]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Membrane alanyl aminopeptidase]]		[[Category: Membrane alanyl aminopeptidase]]

OCA at 09:36, 24 April 2019

2019-04-24T09:36:05Z

←Older revision		Revision as of 09:36, 24 April 2019
Line 1:		Line 1:

	==Crystal structure of E.coli aminopeptidase N in complex with actinonin==		==Crystal structure of E.coli aminopeptidase N in complex with actinonin==
-	<StructureSection load='4q4e' size='340' side='right' caption='[[4q4e]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='4q4e' size='340' side='right'caption='[[4q4e]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4q4e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q4E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4q4e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q4E FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BB2:ACTINONIN'>BB2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BB2:ACTINONIN'>BB2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4q4i\|4q4i]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4q4i\|4q4i]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">pepN, b0932, JW0915 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] </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=4q4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4e OCA], [http://pdbe.org/4q4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q4e RCSB], [http://www.ebi.ac.uk/pdbsum/4q4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q4e ProSAT]</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=4q4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4e OCA], [http://pdbe.org/4q4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q4e RCSB], [http://www.ebi.ac.uk/pdbsum/4q4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q4e ProSAT]</span></td></tr>
Line 20:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 4q4e" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4q4e" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Ecoli]]
		+	[[Category: Large Structures]]
	[[Category: Membrane alanyl aminopeptidase]]		[[Category: Membrane alanyl aminopeptidase]]
	[[Category: Addlagatta, A]]		[[Category: Addlagatta, A]]

OCA at 17:30, 18 January 2017

2017-01-18T17:30:30Z

←Older revision		Revision as of 17:30, 18 January 2017
Line 1:		Line 1:
		+
	==Crystal structure of E.coli aminopeptidase N in complex with actinonin==		==Crystal structure of E.coli aminopeptidase N in complex with actinonin==
	<StructureSection load='4q4e' size='340' side='right' caption='[[4q4e]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='4q4e' size='340' side='right' caption='[[4q4e]], [[Resolution\|resolution]] 1.90Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4q4i\|4q4i]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4q4i\|4q4i]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] </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=4q4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q4e RCSB], [http://www.ebi.ac.uk/pdbsum/4q4e 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=4q4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4e OCA], [http://pdbe.org/4q4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q4e RCSB], [http://www.ebi.ac.uk/pdbsum/4q4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q4e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4q4e" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:48, 15 April 2015

2015-04-15T12:48:33Z

←Older revision		Revision as of 12:48, 15 April 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal structure of E.coli aminopeptidase N in complex with actinonin==
		+	<StructureSection load='4q4e' size='340' side='right' caption='[[4q4e]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4q4e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q4E FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BB2:ACTINONIN'>BB2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4q4i\|4q4i]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] </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=4q4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q4e RCSB], [http://www.ebi.ac.uk/pdbsum/4q4e PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AMPN_ECOLI AMPN_ECOLI]] Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Actinonin is a pseudotripeptide that displays a high affinity towards metalloproteases including peptide deformylases (PDFs) and M1 family aminopeptidases. PDF and M1 family aminopeptidases belong to thermolysin-metzincin superfamily. One of the major differences in terms of substrate binding pockets between these families is presence (in M1 aminopeptidases) or absence (in PDFs) of an S1 substrate pocket. The binding mode of actinonin to PDFs has been established previously; however, it is not clear how the actinonin, without a P1 residue, would bind to the M1 aminopeptidases. Here we describe the crystal structure of Escherichia coli aminopeptidase N (ePepN), a model protein of the M1 family aminopeptidases in complex with actinonin. For comparison we have also determined the structure of ePepN in complex with a well-known tetrapeptide inhibitor, amastatin. From the comparison of the actinonin and amastatin ePepN complexes, it is clear that the P1 residue is not critical as long as strong metal chelating head groups, like hydroxamic acid or alpha-hydroxy ketone, are present. Results from this study will be useful for the design of selective and efficient hydroxamate inhibitors against M1 family aminopeptidases.

-	~~The entry 4q4e is ON HOLD until Apr 14 2016~~	+	Structural basis for the inhibition of M1 family aminopeptidases by the natural product actinonin: Crystal structure in complex with E. coli aminopeptidase N.,Ganji RJ, Reddi R, Gumpena R, Marapaka AK, Arya T, Sankoju P, Bhukya S, Addlagatta A Protein Sci. 2015 Feb 2. doi: 10.1002/pro.2653. PMID:25644575<ref>PMID:25644575</ref>

-	~~Authors: Reddi~~, R.~~, Ganji, R~~.~~J., Addlagatta, A~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: Crystal structure of E.coli aminopeptidase N in complex with actinonin~~	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Membrane alanyl aminopeptidase]]
	[[Category: Addlagatta, A]]		[[Category: Addlagatta, A]]
-	[[Category: Ganji, R.J]]	+	[[Category: Ganji, R J]]
	[[Category: Reddi, R]]		[[Category: Reddi, R]]
		+	[[Category: Aminopeptidase]]
		+	[[Category: Hydrolase]]

OCA at 15:25, 24 December 2014

2014-12-24T15:25:14Z

←Older revision		Revision as of 15:25, 24 December 2014
Line 6:		Line 6:

	Description: Crystal structure of E.coli aminopeptidase N in complex with actinonin		Description: Crystal structure of E.coli aminopeptidase N in complex with actinonin
		+	[[Category: Unreleased Structures]]
		+	[[Category: Addlagatta, A]]
		+	[[Category: Ganji, R.J]]
		+	[[Category: Reddi, R]]

OCA at 08:00, 11 June 2014

2014-06-11T08:00:35Z

←Older revision		Revision as of 08:00, 11 June 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4q4e is ON HOLD until ~~Paper Publication~~	+	The entry 4q4e is ON HOLD until Apr 14 2016

	Authors: Reddi, R., Ganji, R.J., Addlagatta, A.		Authors: Reddi, R., Ganji, R.J., Addlagatta, A.

	Description: Crystal structure of E.coli aminopeptidase N in complex with actinonin		Description: Crystal structure of E.coli aminopeptidase N in complex with actinonin

OCA at 04:57, 4 June 2014

2014-06-04T04:57:13Z

←Older revision		Revision as of 04:57, 4 June 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4q4e is ON HOLD	+	The entry 4q4e is ON HOLD until Paper Publication

	Authors: Reddi, R., Ganji, R.J., Addlagatta, A.		Authors: Reddi, R., Ganji, R.J., Addlagatta, A.

	Description: Crystal structure of E.coli aminopeptidase N in complex with actinonin		Description: Crystal structure of E.coli aminopeptidase N in complex with actinonin

OCA: Protected "4q4e" [edit=sysop:move=sysop]

2014-04-23T07:29:36Z

Protected "4q4e" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:29, 23 April 2014