3uf8 - Revision history

OCA at 10:23, 1 March 2024

OCA — Fri, 01 Mar 2024 10:23:04 GMT

←Older revision		Revision as of 10:23, 1 March 2024
Line 3:		Line 3:
	<StructureSection load='3uf8' size='340' side='right'caption='[[3uf8]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='3uf8' size='340' side='right'caption='[[3uf8]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3uf8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Burp1 Burp1~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UF8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3uf8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei_1710b Burkholderia pseudomallei 1710b] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UF8 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=FK5:8-DEETHYL-8~~-[~~BUT-3-ENYL]-ASCOMYCIN'>FK5</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]] 1.5Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[~~[Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[2keo\|2keo]], [[2l2s\|2l2s]], [[2ko7\|2ko7]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>BURPS1710b_A0907, SMT3, YDR510W, D9719.15 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id~~=320372 BURP1])</td></tr>~~	+
-	~~<tr id='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[https~~:~~//en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number~~ [~~https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8~~] </~~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=3uf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uf8 OCA], [https://pdbe.org/3uf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uf8 RCSB], [https://www.ebi.ac.uk/pdbsum/3uf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uf8 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=3uf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uf8 OCA], [https://pdbe.org/3uf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uf8 RCSB], [https://www.ebi.ac.uk/pdbsum/3uf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uf8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST]] Not known; suppressor of MIF2 mutations.	+	[https://www.uniprot.org/uniprot/Q3JK38_BURP1 Q3JK38_BURP1] [https://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST] Not known; suppressor of MIF2 mutations.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Macrophage infectivity potentiators (Mips) are immunophilin proteins and essential virulence factors for a range of pathogenic organisms. We applied a structural biology approach to characterize a Mip from Burkholderia pseudomallei (BpML1), the causative agent of melioidosis. Crystal structure and nuclear magnetic resonance analyses of BpML1 in complex with known macrocyclics and other derivatives led to the identification of a key chemical scaffold. This scaffold possesses inhibitory potency for BpML1 without the immunosuppressive components of related macrocyclic agents. Biophysical characterization of a compound series with this scaffold allowed binding site specificity in solution and potency determinations for rank ordering the set. The best compounds in this series possessed a low-micromolar affinity for BpML1, bound at the site of enzymatic activity, and inhibited a panel of homologous Mip proteins from other pathogenic bacteria, without demonstrating toxicity in human macrophages. Importantly, the in vitro activity of BpML1 was reduced by these compounds, leading to decreased macrophage infectivity and intracellular growth of Burkholderia pseudomallei. These compounds offer the potential for activity against a new class of antimicrobial targets and present the utility of a structure-based approach for novel antimicrobial drug discovery.	+
-		+
-	A structural biology approach enables the development of antimicrobials targeting bacterial immunophilins.,Begley DW, Fox D 3rd, Jenner D, Juli C, Pierce PG, Abendroth J, Muruthi M, Safford K, Anderson V, Atkins K, Barnes SR, Moen SO, Raymond AC, Stacy R, Myler PJ, Staker BL, Harmer NJ, Norville IH, Holzgrabe U, Sarkar-Tyson M, Edwards TE, Lorimer DD Antimicrob Agents Chemother. 2014 Mar;58(3):1458-67. doi: 10.1128/AAC.01875-13., Epub 2013 Dec 23. PMID:24366729<ref>PMID:24366729</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3uf8" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Burp1~~]]	+	[[Category: Burkholderia pseudomallei 1710b]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Peptidylprolyl isomerase]]~~	+	[[Category: Saccharomyces cerevisiae S288C]]
-	~~[[Category: Structural genomic]]~~	+
-	~~[[Category: Isomerase]]~~	+
-	~~[[Category: Protein binding]]~~	+
-	~~[[Category: Ssgcid~~]]	+

OCA at 06:10, 13 July 2022

OCA — Wed, 13 Jul 2022 06:10:45 GMT

←Older revision		Revision as of 06:10, 13 July 2022
Line 1:		Line 1:

	==Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with a G95A surface mutation from Burkholderia pseudomallei complexed with FK506==		==Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with a G95A surface mutation from Burkholderia pseudomallei complexed with FK506==
-	<StructureSection load='3uf8' size='340' side='right' caption='[[3uf8]], [[Resolution\|resolution]] 1.50Å' scene=''>	+	<StructureSection load='3uf8' size='340' side='right'caption='[[3uf8]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3uf8]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Burp1 Burp1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UF8 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3UF8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3uf8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Burp1 Burp1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UF8 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2keo\|2keo]], [[2l2s\|2l2s]], [[2ko7\|2ko7]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2keo\|2keo]], [[2l2s\|2l2s]], [[2ko7\|2ko7]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BURPS1710b_A0907, SMT3, YDR510W, D9719.15 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=320372 BURP1])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BURPS1710b_A0907, SMT3, YDR510W, D9719.15 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=320372 BURP1])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=3uf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uf8 OCA], [~~http~~://pdbe.org/3uf8 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3uf8 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3uf8 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3uf8 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=3uf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uf8 OCA], [https://pdbe.org/3uf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uf8 RCSB], [https://www.ebi.ac.uk/pdbsum/3uf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uf8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST]] Not known; suppressor of MIF2 mutations.	+	[[https://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST]] Not known; suppressor of MIF2 mutations.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Burp1]]		[[Category: Burp1]]
		+	[[Category: Large Structures]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Structural genomic]]		[[Category: Structural genomic]]

OCA at 18:36, 4 August 2016

OCA — Thu, 04 Aug 2016 18:36:25 GMT

←Older revision		Revision as of 18:36, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with a G95A surface mutation from Burkholderia pseudomallei complexed with FK506==		==Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with a G95A surface mutation from Burkholderia pseudomallei complexed with FK506==
	<StructureSection load='3uf8' size='340' side='right' caption='[[3uf8]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='3uf8' size='340' side='right' caption='[[3uf8]], [[Resolution\|resolution]] 1.50Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BURPS1710b_A0907, SMT3, YDR510W, D9719.15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=320372 BURP1])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BURPS1710b_A0907, SMT3, YDR510W, D9719.15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=320372 BURP1])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=3uf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uf8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uf8 RCSB], [http://www.ebi.ac.uk/pdbsum/3uf8 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=3uf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uf8 OCA], [http://pdbe.org/3uf8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3uf8 RCSB], [http://www.ebi.ac.uk/pdbsum/3uf8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3uf8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 3uf8" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:58, 25 December 2014

OCA — Thu, 25 Dec 2014 11:58:30 GMT

←Older revision		Revision as of 11:58, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3uf8\| PDB=3uf8 \| SCENE= }}~~	+	==Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with a G95A surface mutation from Burkholderia pseudomallei complexed with FK506==
-	===Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with a G95A surface mutation from Burkholderia pseudomallei complexed with FK506===	+	<StructureSection load='3uf8' size='340' side='right' caption='[[3uf8]], [[Resolution\|resolution]] 1.50Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24366729}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3uf8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Burp1 Burp1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UF8 FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2keo\|2keo]], [[2l2s\|2l2s]], [[2ko7\|2ko7]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BURPS1710b_A0907, SMT3, YDR510W, D9719.15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=320372 BURP1])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=3uf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uf8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uf8 RCSB], [http://www.ebi.ac.uk/pdbsum/3uf8 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST]] Not known; suppressor of MIF2 mutations.		[[http://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST]] Not known; suppressor of MIF2 mutations.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Macrophage infectivity potentiators (Mips) are immunophilin proteins and essential virulence factors for a range of pathogenic organisms. We applied a structural biology approach to characterize a Mip from Burkholderia pseudomallei (BpML1), the causative agent of melioidosis. Crystal structure and nuclear magnetic resonance analyses of BpML1 in complex with known macrocyclics and other derivatives led to the identification of a key chemical scaffold. This scaffold possesses inhibitory potency for BpML1 without the immunosuppressive components of related macrocyclic agents. Biophysical characterization of a compound series with this scaffold allowed binding site specificity in solution and potency determinations for rank ordering the set. The best compounds in this series possessed a low-micromolar affinity for BpML1, bound at the site of enzymatic activity, and inhibited a panel of homologous Mip proteins from other pathogenic bacteria, without demonstrating toxicity in human macrophages. Importantly, the in vitro activity of BpML1 was reduced by these compounds, leading to decreased macrophage infectivity and intracellular growth of Burkholderia pseudomallei. These compounds offer the potential for activity against a new class of antimicrobial targets and present the utility of a structure-based approach for novel antimicrobial drug discovery.

-	~~==About this Structure==~~	+	A structural biology approach enables the development of antimicrobials targeting bacterial immunophilins.,Begley DW, Fox D 3rd, Jenner D, Juli C, Pierce PG, Abendroth J, Muruthi M, Safford K, Anderson V, Atkins K, Barnes SR, Moen SO, Raymond AC, Stacy R, Myler PJ, Staker BL, Harmer NJ, Norville IH, Holzgrabe U, Sarkar-Tyson M, Edwards TE, Lorimer DD Antimicrob Agents Chemother. 2014 Mar;58(3):1458-67. doi: 10.1128/AAC.01875-13., Epub 2013 Dec 23. PMID:24366729<ref>PMID:24366729</ref>
-	~~[[3uf8]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Burp1 Burp1]~~. ~~Full crystallographic information is available from [http~~:/~~/oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=3UF8 OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024366729</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Burp1]]		[[Category: Burp1]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
-	[[Category: ~~SSGCID, Seattle~~ Structural ~~Genomics Center for Infectious Disease.~~]]	+	[[Category: Structural genomic]]
	[[Category: Isomerase]]		[[Category: Isomerase]]
	[[Category: Protein binding]]		[[Category: Protein binding]]
-	[[Category: Seattle structural genomics center for infectious disease]]
	[[Category: Ssgcid]]		[[Category: Ssgcid]]

OCA at 13:41, 12 March 2014

OCA — Wed, 12 Mar 2014 13:41:20 GMT

←Older revision		Revision as of 13:41, 12 March 2014
Line 1:		Line 1:
-	[[Image:3uf8.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3uf8", 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_3uf8\| PDB=3uf8 \| SCENE= }}		{{STRUCTURE_3uf8\| PDB=3uf8 \| SCENE= }}
-
	===Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with a G95A surface mutation from Burkholderia pseudomallei complexed with FK506===		===Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with a G95A surface mutation from Burkholderia pseudomallei complexed with FK506===
		+	{{ABSTRACT_PUBMED_24366729}}

		+	==Function==
		+	[[http://www.uniprot.org/uniprot/SMT3_YEAST SMT3_YEAST]] Not known; suppressor of MIF2 mutations.

	==About this Structure==		==About this Structure==
-	[[3uf8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Burkholderia_pseudomallei,_saccharomyces_cerevisiae Burkholderia pseudomallei, saccharomyces cerevisiae~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UF8 OCA].	+	[[3uf8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Burp1 Burp1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UF8 OCA].
-	[[Category: ~~Burkholderia pseudomallei, saccharomyces cerevisiae~~]]	+
		+	==Reference==
		+	<ref group="xtra">PMID:024366729</ref><references group="xtra"/><references/>
		+	[[Category: Burp1]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: SSGCID, Seattle Structural Genomics Center for Infectious Disease.]]		[[Category: SSGCID, Seattle Structural Genomics Center for Infectious Disease.]]

OCA at 05:31, 30 November 2011

OCA — Wed, 30 Nov 2011 05:31:46 GMT

←Older revision		Revision as of 05:31, 30 November 2011
Line 1:		Line 1:
-	[[Image:3uf8.~~jpg~~\|left\|200px]]	+	[[Image:3uf8.png\|left\|200px]]

	<!--		<!--
Line 9:		Line 9:
	{{STRUCTURE_3uf8\| PDB=3uf8 \| SCENE= }}		{{STRUCTURE_3uf8\| PDB=3uf8 \| SCENE= }}

-	===Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei complexed with FK506===	+	===Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with a G95A surface mutation from Burkholderia pseudomallei complexed with FK506===

OCA: Protected "3uf8" [edit=sysop:move=sysop]

OCA — Wed, 09 Nov 2011 11:54:48 GMT

Protected "3uf8" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:54, 9 November 2011