4idy - Revision history

OCA at 09:03, 9 November 2022

2022-11-09T09:03:38Z

←Older revision		Revision as of 09:03, 9 November 2022
Line 1:		Line 1:

	==Mycobacterium Tuberculosis Methionine aminopeptidase Type 1c in complex with 2-hydroxyethyl disulfide==		==Mycobacterium Tuberculosis Methionine aminopeptidase Type 1c in complex with 2-hydroxyethyl disulfide==
-	<StructureSection load='4idy' size='340' side='right' caption='[[4idy]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='4idy' size='340' side='right'caption='[[4idy]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4idy]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus~~ tuberculosis~~" (zopf 1883) klein 1884~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IDY OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4IDY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4idy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IDY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IDY FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
-	~~<tr~~ id~~='NonStdRes'><td class~~="~~sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat~~"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</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=4idy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4idy OCA], [https://pdbe.org/4idy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4idy RCSB], [https://www.ebi.ac.uk/pdbsum/4idy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4idy ProSAT]</span></td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b~~></td>~~<td class="sblockDat">[[1yj3\|1yj3]]~~, ~~[[4iec\|4iec]], [[4if7\|4if7]]~~<~~/td></tr>~~	+
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b></td><td class="sblockDat">map ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>~~	+
-	~~<tr id='activity~~'>~~<td class="sblockLbl"><b>Activity:~~</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </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=4idy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4idy OCA], [~~http~~://pdbe.org/4idy PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4idy RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4idy PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4idy ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/~~AMPM2_MYCTU AMPM2_MYCTU]~~] Removes the N-terminal methionine from nascent proteins~~, when the penultimate amino acid~~ is ~~alanine or proline, but enzyme activity is remarkably low~~ when the second residue is ~~phenylalanine~~ or ~~leucine~~. ~~With glycine at~~ the ~~second position, Map is more active with a tetrapeptide than with a tripeptide~~.<ref>PMID:19688379</ref> <ref>PMID:20038112</ref>	+	[https://www.uniprot.org/uniprot/MAP12_MYCTU MAP12_MYCTU] Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.[HAMAP-Rule:MF_01974]<ref>PMID:19688379</ref> <ref>PMID:20038112</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 20:

	==See Also==		==See Also==
-	*[[Aminopeptidase\|Aminopeptidase]]	+	*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Methionyl aminopeptidase~~]]	+	[[Category: Large Structures]]
-	[[Category: Addlagatta, A]]	+	[[Category: Mycobacterium tuberculosis]]
-	[[Category: Gumpena, R]]	+	[[Category: Addlagatta A]]
-	[[Category: Kishor, C]]	+	[[Category: Gumpena R]]
-	[[Category: Reddi, R]]	+	[[Category: Kishor C]]
-	~~[[Category: 2-hydroxyethylcysteine disulfide]]~~	+	[[Category: Reddi R]]
-	~~[[Category: Aminopeptidase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Pita-bread fold~~]]	+

OCA at 21:23, 11 August 2016

2016-08-11T21:23:45Z

←Older revision		Revision as of 21:23, 11 August 2016
Line 1:		Line 1:
		+
	==Mycobacterium Tuberculosis Methionine aminopeptidase Type 1c in complex with 2-hydroxyethyl disulfide==		==Mycobacterium Tuberculosis Methionine aminopeptidase Type 1c in complex with 2-hydroxyethyl disulfide==
	<StructureSection load='4idy' size='340' side='right' caption='[[4idy]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4idy' size='340' side='right' caption='[[4idy]], [[Resolution\|resolution]] 2.00Å' scene=''>
Line 8:		Line 9:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">map ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">map ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </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=4idy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4idy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4idy RCSB], [http://www.ebi.ac.uk/pdbsum/4idy 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=4idy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4idy OCA], [http://pdbe.org/4idy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4idy RCSB], [http://www.ebi.ac.uk/pdbsum/4idy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4idy ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 20:		Line 21:
	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 4idy" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 10:33, 7 February 2015

2015-02-07T10:33:38Z

←Older revision		Revision as of 10:33, 7 February 2015
Line 12:		Line 12:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/AMPM2_MYCTU AMPM2_MYCTU]] Removes the N-terminal methionine from nascent proteins, when the penultimate amino acid is alanine or proline, but enzyme activity is remarkably low when the second residue is phenylalanine or leucine. With glycine at the second position, Map is more active with a tetrapeptide than with a tripeptide.<ref>PMID:19688379</ref> <ref>PMID:20038112</ref>		[[http://www.uniprot.org/uniprot/AMPM2_MYCTU AMPM2_MYCTU]] Removes the N-terminal methionine from nascent proteins, when the penultimate amino acid is alanine or proline, but enzyme activity is remarkably low when the second residue is phenylalanine or leucine. With glycine at the second position, Map is more active with a tetrapeptide than with a tripeptide.<ref>PMID:19688379</ref> <ref>PMID:20038112</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Methionine aminopeptidases (MetAPs) cleave initiator methionine from ~ 70% of the newly synthesized proteins in every living cell, and specific inhibition or knockdown of this function is detrimental. MetAPs are metalloenzymes, and are broadly classified into two subtypes, type I and type II. Bacteria contain only type I MetAPs, and the active site of these enzymes contains a conserved cysteine. By contrast, in type II enzymes the analogous position is occupied by a conserved glycine. Here, we report the reactivity of the active site cysteine in a type I MetAP, MetAP1c, of Mycobacterium tuberculosis (MtMetAP1c) towards highly selective cysteine-specific reagents. The authenticity of selective modification of Cys105 of MtMetAP1c was established by using site-directed mutagenesis and crystal structure determination of covalent and noncovalent complexes. On the basis of these observations, we propose that metal ions in the active site assist in the covalent modification of Cys105 by orienting the reagents appropriately for a successful reaction. These studies establish, for the first time, that the conserved cysteine of type I MetAPs can be targeted for selective inhibition, and we believe that this chemistry can be exploited for further drug discovery efforts regarding microbial MetAPs.
		+
		+	Selective targeting of the conserved active site cysteine of Mycobacterium tuberculosis methionine aminopeptidase with electrophilic reagents.,Reddi R, Arya T, Kishor C, Gumpena R, Ganji RJ, Bhukya S, Addlagatta A FEBS J. 2014 Sep;281(18):4240-8. doi: 10.1111/febs.12847. Epub 2014 Jun 6. PMID:24841365<ref>PMID:24841365</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==

OCA at 22:51, 25 December 2014

2014-12-25T22:51:07Z

←Older revision		Revision as of 22:51, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4idy\| PDB=4idy \| SCENE= }}~~	+	==Mycobacterium Tuberculosis Methionine aminopeptidase Type 1c in complex with 2-hydroxyethyl disulfide==
-	===Mycobacterium Tuberculosis Methionine aminopeptidase Type 1c in complex with 2-hydroxyethyl disulfide===	+	<StructureSection load='4idy' size='340' side='right' caption='[[4idy]], [[Resolution\|resolution]] 2.00Å' scene=''>
-		+	== Structural highlights ==
-	==Function==	+	<table><tr><td colspan='2'>[[4idy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IDY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IDY FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yj3\|1yj3]], [[4iec\|4iec]], [[4if7\|4if7]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">map ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </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=4idy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4idy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4idy RCSB], [http://www.ebi.ac.uk/pdbsum/4idy PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/AMPM2_MYCTU AMPM2_MYCTU]] Removes the N-terminal methionine from nascent proteins, when the penultimate amino acid is alanine or proline, but enzyme activity is remarkably low when the second residue is phenylalanine or leucine. With glycine at the second position, Map is more active with a tetrapeptide than with a tripeptide.<ref>PMID:19688379</ref> <ref>PMID:20038112</ref>		[[http://www.uniprot.org/uniprot/AMPM2_MYCTU AMPM2_MYCTU]] Removes the N-terminal methionine from nascent proteins, when the penultimate amino acid is alanine or proline, but enzyme activity is remarkably low when the second residue is phenylalanine or leucine. With glycine at the second position, Map is more active with a tetrapeptide than with a tripeptide.<ref>PMID:19688379</ref> <ref>PMID:20038112</ref>

-	==~~About this Structure~~==	+	==See Also==
-	[[~~4idy~~]] ~~is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IDY OCA].~~	+	*[[Aminopeptidase\|Aminopeptidase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Methionyl aminopeptidase]]		[[Category: Methionyl aminopeptidase]]
-	[[Category: Addlagatta, A.]]	+	[[Category: Addlagatta, A]]
-	[[Category: Gumpena, R.]]	+	[[Category: Gumpena, R]]
-	[[Category: Kishor, C.]]	+	[[Category: Kishor, C]]
-	[[Category: Reddi, R.]]	+	[[Category: Reddi, R]]
	[[Category: 2-hydroxyethylcysteine disulfide]]		[[Category: 2-hydroxyethylcysteine disulfide]]
	[[Category: Aminopeptidase]]		[[Category: Aminopeptidase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Pita-bread fold]]		[[Category: Pita-bread fold]]

OCA at 10:36, 18 December 2013

2013-12-18T10:36:13Z

←Older revision		Revision as of 10:36, 18 December 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4idy\| PDB=4idy \| SCENE= }}
		+	===Mycobacterium Tuberculosis Methionine aminopeptidase Type 1c in complex with 2-hydroxyethyl disulfide===

-	~~The entry 4idy~~ is ~~ON HOLD~~ ~~until Dec 13 2014~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/AMPM2_MYCTU AMPM2_MYCTU]] Removes the N-terminal methionine from nascent proteins, when the penultimate amino acid is alanine or proline, but enzyme activity is remarkably low when the second residue is phenylalanine or leucine. With glycine at the second position, Map is more active with a tetrapeptide than with a tripeptide.<ref>PMID:19688379</ref> <ref>PMID:20038112</ref>

-	~~Authors~~: ~~Reddi, R~~.~~, Gumpena, R~~.~~, Kishor, C~~.~~, Addlagatta, A~~.	+	==About this Structure==
		+	[[4idy]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IDY OCA].

-	~~Description~~: ~~Mycobacterium Tuberculosis Methionine~~ aminopeptidase ~~Type 1c in complex with~~ 2-~~hydroxyethyl~~ disulfide	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Methionyl aminopeptidase]]
		+	[[Category: Addlagatta, A.]]
		+	[[Category: Gumpena, R.]]
		+	[[Category: Kishor, C.]]
		+	[[Category: Reddi, R.]]
		+	[[Category: 2-hydroxyethylcysteine disulfide]]
		+	[[Category: Aminopeptidase]]
		+	[[Category: Hydrolase]]
		+	[[Category: Pita-bread fold]]

OCA at 09:51, 13 March 2013

2013-03-13T09:51:53Z

←Older revision		Revision as of 09:51, 13 March 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4idy is ON HOLD	+	The entry 4idy is ON HOLD until Dec 13 2014

	Authors: Reddi, R., Gumpena, R., Kishor, C., Addlagatta, A.		Authors: Reddi, R., Gumpena, R., Kishor, C., Addlagatta, A.

	Description: Mycobacterium Tuberculosis Methionine aminopeptidase Type 1c in complex with 2-hydroxyethyl disulfide		Description: Mycobacterium Tuberculosis Methionine aminopeptidase Type 1c in complex with 2-hydroxyethyl disulfide

OCA at 08:55, 2 January 2013

2013-01-02T08:55:52Z

←Older revision		Revision as of 08:55, 2 January 2013
Line 3:		Line 3:
	The entry 4idy is ON HOLD		The entry 4idy is ON HOLD

-	Authors: ~~Ravikumar~~ Reddi, ~~Rajesh~~ Gumpena, ~~Chandan~~ Kishor, ~~Anthony~~ Addlagatta	+	Authors: Reddi, R., Gumpena, R., Kishor, C., Addlagatta, A.

	Description: Mycobacterium Tuberculosis Methionine aminopeptidase Type 1c in complex with 2-hydroxyethyl disulfide		Description: Mycobacterium Tuberculosis Methionine aminopeptidase Type 1c in complex with 2-hydroxyethyl disulfide

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

2012-12-19T11:08:44Z

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

←Older revision

Revision as of 11:08, 19 December 2012

OCA: New page: '''Unreleased structure''' The entry 4idy is ON HOLD Authors: Ravikumar Reddi, Rajesh Gumpena, Chandan Kishor, Anthony Addlagatta Description: Mycobacterium Tuberculosis Methionine ami...

2012-12-19T11:08:43Z

New page: '''Unreleased structure''' The entry 4idy is ON HOLD Authors: Ravikumar Reddi, Rajesh Gumpena, Chandan Kishor, Anthony Addlagatta Description: Mycobacterium Tuberculosis Methionine ami...

New page

'''Unreleased structure'''

The entry 4idy is ON HOLD

Authors: Ravikumar Reddi, Rajesh Gumpena, Chandan Kishor, Anthony Addlagatta

Description: Mycobacterium Tuberculosis Methionine aminopeptidase Type 1c in complex with 2-hydroxyethyl disulfide