2hyp - Revision history

OCA at 09:00, 21 February 2024

2024-02-21T09:00:36Z

← Older revision		Revision as of 09:00, 21 February 2024
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	<StructureSection load='2hyp' size='340' side='right'caption='[[2hyp]], [[Resolution\|resolution]] 2.05Å' scene=''>		<StructureSection load='2hyp' size='340' side='right'caption='[[2hyp]], [[Resolution\|resolution]] 2.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2hyp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Myctu Myctu~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HYP FirstGlance]. <br>		<table><tr><td colspan='2'>[[2hyp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HYP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 2.05Å</td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hy1\|2hy1]], [[2hyo\|2hyo]]</div></td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">icc ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>~~
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3',5'-cyclic-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17] </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=2hyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hyp OCA], [https://pdbe.org/2hyp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hyp RCSB], [https://www.ebi.ac.uk/pdbsum/2hyp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hyp 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=2hyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hyp OCA], [https://pdbe.org/2hyp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hyp RCSB], [https://www.ebi.ac.uk/pdbsum/2hyp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hyp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/~~CPDA_MYCTO CPDA_MYCTO~~]~~] Hydrolyzes~~ cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes. May play a role in pathogenicity, not only by hydrolyzing cAMP, but also by altering properties of the cell wall (~~By similarity~~).~~[HAMAP~~-~~Rule~~:~~MF_00905]~~		[https://www.uniprot.org/uniprot/CNPD3_MYCTU CNPD3_MYCTU] Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP (PubMed:16313172, PubMed:18757371). Can use 2',3'-cAMP, 2',3'-cGMP, 3',5'-cAMP, 3',5'-cGMP and 3',5'-cUMP (PubMed:16313172, PubMed:18757371, PubMed:19801656). Hydrolysis of 2',3'-cAMP produces a mixture of 3'-AMP (major product) and 2'-AMP (minor product) (PubMed:18757371). In vitro, is 150-fold more active in hydrolyzing 2',3'-cAMP than 3',5'-cAMP (PubMed:18757371). Can also hydrolyze the model substrates p-nitrophenyl phosphate (pNPP), bis-(p-nitrophenyl phosphate) (bis(pNPP)) and p-nitrophenyl phenylphosphonate (pNPPP) (PubMed:16313172, PubMed:18757371, PubMed:19801656). Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes (PubMed:16313172). May play a role in pathogenicity, not only by hydrolyzing cAMP, but also by altering properties of the cell wall (PubMed:19801656).<ref>PMID:16313172</ref> <ref>PMID:18757371</ref> <ref>PMID:19801656</ref> Overexpression elicits a transcriptional response that is independent of the phosphodiesterase activity. It does not alter the levels of cAMP-CRP regulated genes, even though cAMP levels are reduced in cells.<ref>PMID:23835087</ref>
	== 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=2hyp 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=2hyp ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Cyclic nucleotide monophosphate (cNMP) hydrolysis in bacteria and eukaryotes is brought about by distinct cNMP phosphodiesterases (PDEs). Since these enzymes differ in amino acid sequence and properties, they have evolved by convergent evolution. Cyclic NMP PDEs cleave cNMPs to NMPs, and the Rv0805 gene product is, to date, the only identifiable cNMP PDE in the genome of Mycobacterium tuberculosis. We have shown that Rv0805 is a cAMP/cGMP dual specificity PDE, and is unrelated in amino acid sequence to the mammalian cNMP PDEs. Rv0805 is a dimeric, Fe(3+)-Mn(2+) binuclear PDE, and mutational analysis demonstrated that the active site metals are co-ordinated by conserved aspartate, histidine and asparagine residues. We report here the structure of the catalytic core of Rv0805, which is distantly related to the calcineurin-like phosphatases. The crystal structure of the Rv0805 dimer shows that the active site metals contribute to dimerization and thus play an additional structural role apart from their involvement in catalysis. We also present the crystal structures of the Asn97Ala mutant protein that lacks one of the Mn(2+) co-ordinating residues as well as the Asp66Ala mutant that has a compromised cAMP hydrolytic activity, providing a structural basis for the catalytic properties of these mutant proteins. A molecule of phosphate is bound in a bidentate manner at the active site of the Rv0805 wild-type protein, and cacodylate occupies a similar position in the crystal structure of the Asp66Ala mutant protein. A unique substrate binding pocket in Rv0805 was identified by computational docking studies, and the role of the His140 residue in interacting with cAMP was validated through mutational analysis. This report on the first structure of a bacterial cNMP PDE thus significantly extends our molecular understanding of cAMP hydrolysis in class III PDEs.

	Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis.,Shenoy AR, Capuder M, Draskovic P, Lamba D, Visweswariah SS, Podobnik M J Mol Biol. 2007 Jan 5;365(1):211-25. Epub 2006 Oct 6. PMID:17059828<ref>PMID:17059828</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 2hyp" style="background-color:#fffaf0;"></div>~~
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Myctu~~]]		[[Category: Mycobacterium tuberculosis H37Rv]]
	[[Category: Capuder, M]]		[[Category: Capuder M]]
	[[Category: Draskovic, P]]		[[Category: Draskovic P]]
	[[Category: Lamba, D]]		[[Category: Lamba D]]
	[[Category: Podobnik, M]]		[[Category: Podobnik M]]
	[[Category: Shenoy~~, A R~~]]		[[Category: Shenoy AR]]
	[[Category: Visweswariah~~, S S]]~~		[[Category: Visweswariah SS]]
	~~[[Category: Bi-nuclear active site]]~~
	~~[[Category: Camp]]~~
	~~[[Category: Hydrolase]]~~
	~~[[Category: Metallophosphoesterase]]~~
	~~[[Category: Phosphodiesterase~~]]

OCA at 07:24, 24 March 2021

2021-03-24T07:24:40Z

← Older revision		Revision as of 07:24, 24 March 2021
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	==Crystal structure of Rv0805 D66A mutant==		==Crystal structure of Rv0805 D66A mutant==
	<StructureSection load='2hyp' size='340' side='right' caption='[[2hyp]], [[Resolution\|resolution]] 2.05Å' scene=''>		<StructureSection load='2hyp' size='340' side='right'caption='[[2hyp]], [[Resolution\|resolution]] 2.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2hyp]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HYP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2HYP FirstGlance]. <br>		<table><tr><td colspan='2'>[[2hyp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HYP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hy1\|2hy1]], [[2hyo\|2hyo]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hy1\|2hy1]], [[2hyo\|2hyo]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">icc ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">icc ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/3',5'-cyclic-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3',5'-cyclic-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17] </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=2hyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hyp OCA], [~~http~~://pdbe.org/2hyp PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2hyp RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2hyp PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2hyp 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=2hyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hyp OCA], [https://pdbe.org/2hyp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hyp RCSB], [https://www.ebi.ac.uk/pdbsum/2hyp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hyp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/CPDA_MYCTO CPDA_MYCTO]] Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes. May play a role in pathogenicity, not only by hydrolyzing cAMP, but also by altering properties of the cell wall (By similarity).[HAMAP-Rule:MF_00905]		[[https://www.uniprot.org/uniprot/CPDA_MYCTO CPDA_MYCTO]] Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes. May play a role in pathogenicity, not only by hydrolyzing cAMP, but also by altering properties of the cell wall (By similarity).[HAMAP-Rule:MF_00905]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hy/2hyp_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hy/2hyp_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>
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	</StructureSection>		</StructureSection>
	[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]		[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]
			[[Category: Large Structures]]
	[[Category: Myctu]]		[[Category: Myctu]]
	[[Category: Capuder, M]]		[[Category: Capuder, M]]

OCA at 08:19, 18 October 2017

2017-10-18T08:19:28Z

← Older revision		Revision as of 08:19, 18 October 2017
Line 1:		Line 1:

	==Crystal structure of Rv0805 D66A mutant==		==Crystal structure of Rv0805 D66A mutant==
	<StructureSection load='2hyp' size='340' side='right' caption='[[2hyp]], [[Resolution\|resolution]] 2.05Å' scene=''>		<StructureSection load='2hyp' size='340' side='right' caption='[[2hyp]], [[Resolution\|resolution]] 2.05Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">icc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">icc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3',5'-cyclic-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3',5'-cyclic-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17] </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=2hyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hyp OCA], [http://pdbe.org/2hyp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hyp RCSB], [http://www.ebi.ac.uk/pdbsum/2hyp 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=2hyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hyp OCA], [http://pdbe.org/2hyp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hyp RCSB], [http://www.ebi.ac.uk/pdbsum/2hyp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hyp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	<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=2hyp ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 13:55, 11 September 2015

2015-09-11T13:55:57Z

← Older revision		Revision as of 13:55, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2hyp' size='340' side='right' caption='[[2hyp]], [[Resolution\|resolution]] 2.05Å' scene=''>		<StructureSection load='2hyp' size='340' side='right' caption='[[2hyp]], [[Resolution\|resolution]] 2.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2hyp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mycobacterium_tuberculosis_h37rv Mycobacterium tuberculosis h37rv~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HYP FirstGlance]. <br>		<table><tr><td colspan='2'>[[2hyp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HYP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hy1\|2hy1]], [[2hyo\|2hyo]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hy1\|2hy1]], [[2hyo\|2hyo]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">icc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 ~~Mycobacterium tuberculosis H37Rv~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">icc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3',5'-cyclic-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3',5'-cyclic-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17] </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=2hyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hyp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hyp RCSB], [http://www.ebi.ac.uk/pdbsum/2hyp 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=2hyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hyp OCA], [http://pdbe.org/2hyp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hyp RCSB], [http://www.ebi.ac.uk/pdbsum/2hyp PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/CPDA_MYCTO CPDA_MYCTO]] Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes. May play a role in pathogenicity, not only by hydrolyzing cAMP, but also by altering properties of the cell wall (By similarity).[HAMAP-Rule:MF_00905]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 27:		Line 29:
	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 2hyp" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 32:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]		[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]
	[[Category: ~~Mycobacterium tuberculosis h37rv~~]]		[[Category: Myctu]]
	[[Category: Capuder, M]]		[[Category: Capuder, M]]
	[[Category: Draskovic, P]]		[[Category: Draskovic, P]]

OCA at 08:28, 16 January 2015

2015-01-16T08:28:13Z

← Older revision		Revision as of 08:28, 16 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2hyp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_h37rv Mycobacterium tuberculosis h37rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HYP FirstGlance]. <br>		<table><tr><td colspan='2'>[[2hyp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_h37rv Mycobacterium tuberculosis h37rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HYP FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hy1\|2hy1]], [[2hyo\|2hyo]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hy1\|2hy1]], [[2hyo\|2hyo]]</td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">icc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 Mycobacterium tuberculosis H37Rv])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">icc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 Mycobacterium tuberculosis H37Rv])</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3',5'-cyclic-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3',5'-cyclic-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17] </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=2hyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hyp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hyp RCSB], [http://www.ebi.ac.uk/pdbsum/2hyp 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=2hyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hyp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hyp RCSB], [http://www.ebi.ac.uk/pdbsum/2hyp 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 33:		Line 33:
	[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]		[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]
	[[Category: Mycobacterium tuberculosis h37rv]]		[[Category: Mycobacterium tuberculosis h37rv]]
	[[Category: Capuder, M.]]		[[Category: Capuder, M]]
	[[Category: Draskovic, P.]]		[[Category: Draskovic, P]]
	[[Category: Lamba, D.]]		[[Category: Lamba, D]]
	[[Category: Podobnik, M.]]		[[Category: Podobnik, M]]
	[[Category: Shenoy, A R.]]		[[Category: Shenoy, A R]]
	[[Category: Visweswariah, S S.]]		[[Category: Visweswariah, S S]]
	[[Category: Bi-nuclear active site]]		[[Category: Bi-nuclear active site]]
	[[Category: Camp]]		[[Category: Camp]]

OCA at 08:08, 30 September 2014

2014-09-30T08:08:01Z

← Older revision		Revision as of 08:08, 30 September 2014
Line 1:		Line 1:
	[[Image:~~2hyp~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal structure of Rv0805 D66A mutant==
			<StructureSection load='2hyp' size='340' side='right' caption='[[2hyp]], [[Resolution\|resolution]] 2.05Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2hyp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_h37rv Mycobacterium tuberculosis h37rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HYP FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hy1\|2hy1]], [[2hyo\|2hyo]]</td></tr>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">icc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 Mycobacterium tuberculosis H37Rv])</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3',5'-cyclic-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17] </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=2hyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hyp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hyp RCSB], [http://www.ebi.ac.uk/pdbsum/2hyp 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/hy/2hyp_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 ==
			Cyclic nucleotide monophosphate (cNMP) hydrolysis in bacteria and eukaryotes is brought about by distinct cNMP phosphodiesterases (PDEs). Since these enzymes differ in amino acid sequence and properties, they have evolved by convergent evolution. Cyclic NMP PDEs cleave cNMPs to NMPs, and the Rv0805 gene product is, to date, the only identifiable cNMP PDE in the genome of Mycobacterium tuberculosis. We have shown that Rv0805 is a cAMP/cGMP dual specificity PDE, and is unrelated in amino acid sequence to the mammalian cNMP PDEs. Rv0805 is a dimeric, Fe(3+)-Mn(2+) binuclear PDE, and mutational analysis demonstrated that the active site metals are co-ordinated by conserved aspartate, histidine and asparagine residues. We report here the structure of the catalytic core of Rv0805, which is distantly related to the calcineurin-like phosphatases. The crystal structure of the Rv0805 dimer shows that the active site metals contribute to dimerization and thus play an additional structural role apart from their involvement in catalysis. We also present the crystal structures of the Asn97Ala mutant protein that lacks one of the Mn(2+) co-ordinating residues as well as the Asp66Ala mutant that has a compromised cAMP hydrolytic activity, providing a structural basis for the catalytic properties of these mutant proteins. A molecule of phosphate is bound in a bidentate manner at the active site of the Rv0805 wild-type protein, and cacodylate occupies a similar position in the crystal structure of the Asp66Ala mutant protein. A unique substrate binding pocket in Rv0805 was identified by computational docking studies, and the role of the His140 residue in interacting with cAMP was validated through mutational analysis. This report on the first structure of a bacterial cNMP PDE thus significantly extends our molecular understanding of cAMP hydrolysis in class III PDEs.

	~~{{STRUCTURE_2hyp\| PDB=2hyp \| SCENE= }}~~		Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis.,Shenoy AR, Capuder M, Draskovic P, Lamba D, Visweswariah SS, Podobnik M J Mol Biol. 2007 Jan 5;365(1):211-25. Epub 2006 Oct 6. PMID:17059828<ref>PMID:17059828</ref>

	~~===Crystal structure~~ of ~~Rv0805 D66A mutant===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_17059828}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[2hyp]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Mycobacterium_tuberculosis_h37rv Mycobacterium tuberculosis h37rv]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2HYP OCA].~~		</StructureSection>

	==~~Reference~~==
	<~~ref group="xtra">PMID:017059828<~~/~~ref><ref group="xtra">PMID:016313172</ref~~><~~references group="xtra"~~/>
	[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]		[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]
	[[Category: Mycobacterium tuberculosis h37rv]]		[[Category: Mycobacterium tuberculosis h37rv]]

OCA at 13:01, 30 January 2013

2013-01-30T13:01:31Z

← Older revision		Revision as of 13:01, 30 January 2013
Line 1:		Line 1:
	[[Image:2hyp.png\|left\|200px]]		[[Image:2hyp.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2hyp", 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.~~
	~~-->~~
	{{STRUCTURE_2hyp\| PDB=2hyp \| SCENE= }}		{{STRUCTURE_2hyp\| PDB=2hyp \| SCENE= }}

	===Crystal structure of Rv0805 D66A mutant===		===Crystal structure of Rv0805 D66A mutant===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_17059828}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 17059828 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_17059828}}		{{ABSTRACT_PUBMED_17059828}}

Line 22:		Line 11:

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~17059828~~</ref><ref group="xtra">PMID:~~16313172~~</ref><references group="xtra"/>		<ref group="xtra">PMID:017059828</ref><ref group="xtra">PMID:016313172</ref><references group="xtra"/>
	[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]		[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]
	[[Category: Mycobacterium tuberculosis h37rv]]		[[Category: Mycobacterium tuberculosis h37rv]]

OCA: Protected "2hyp" [edit=sysop:move=sysop]

2011-03-14T18:52:32Z

Protected "2hyp" [edit=sysop:move=sysop]

← Older revision	Revision as of 18:52, 14 March 2011
(No difference)

OCA at 18:52, 14 March 2011

2011-03-14T18:52:30Z

← Older revision		Revision as of 18:52, 14 March 2011
Line 1:		Line 1:
	~~{{Seed}}~~
	[[Image:2hyp.png\|left\|200px]]		[[Image:2hyp.png\|left\|200px]]

Line 20:		Line 19:

	==About this Structure==		==About this Structure==
	~~2HYP~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/~~Mycobacterium_tuberculosis~~ Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HYP OCA].		[[2hyp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_h37rv Mycobacterium tuberculosis h37rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HYP OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:17059828</ref><ref group="xtra">PMID:16313172</ref><references group="xtra"/>		<ref group="xtra">PMID:17059828</ref><ref group="xtra">PMID:16313172</ref><references group="xtra"/>
	[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]		[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]
	[[Category: Mycobacterium tuberculosis]]		[[Category: Mycobacterium tuberculosis h37rv]]
	[[Category: Capuder, M.]]		[[Category: Capuder, M.]]
	[[Category: Draskovic, P.]]		[[Category: Draskovic, P.]]
Line 34:		Line 33:
	[[Category: Bi-nuclear active site]]		[[Category: Bi-nuclear active site]]
	[[Category: Camp]]		[[Category: Camp]]
			[[Category: Hydrolase]]
	[[Category: Metallophosphoesterase]]		[[Category: Metallophosphoesterase]]
	[[Category: Phosphodiesterase]]		[[Category: Phosphodiesterase]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 00:04:55 2009''~~

OCA at 22:04, 17 February 2009

2009-02-17T22:04:58Z

← Older revision		Revision as of 22:04, 17 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
	2HYP is a ~~[[Single protein]]~~ structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HYP OCA].		2HYP is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HYP OCA].

	==Reference==		==Reference==
	Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis., Shenoy AR, Capuder M, Draskovic P, Lamba D, Visweswariah SS, Podobnik M, J Mol Biol. 2007 Jan 5;365(1):211-25. Epub 2006 Oct 6. PMID:~~[http://www.ncbi.nlm.nih.gov/pubmed~~/~~17059828 17059828]~~		<ref group="xtra">PMID:17059828</ref><ref group="xtra">PMID:16313172</ref><references group="xtra"/>

	The Rv0805 gene from Mycobacterium tuberculosis encodes a 3',5'-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis., Shenoy AR, Sreenath N, Podobnik M, Kovacevic M, Visweswariah SS, Biochemistry. 2005 Dec 6;44(48):15695-704. PMID:~~[http://www.ncbi.nlm.nih.gov~~/~~pubmed~~/~~16313172 16313172]~~
	[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]		[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]
	[[Category: Mycobacterium tuberculosis]]		[[Category: Mycobacterium tuberculosis]]
	~~[[Category: Single protein]]~~
	[[Category: Capuder, M.]]		[[Category: Capuder, M.]]
	[[Category: Draskovic, P.]]		[[Category: Draskovic, P.]]
Line 40:		Line 37:
	[[Category: Phosphodiesterase]]		[[Category: Phosphodiesterase]]

	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Jul 29 07~~:23:~~28 2008~~''		''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 00:04:55 2009''