5gqt - Revision history

OCA at 09:13, 20 March 2024

OCA — Wed, 20 Mar 2024 09:13:31 GMT

←Older revision		Revision as of 09:13, 20 March 2024
Line 9:		Line 9:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/JAL28_ARATH JAL28_ARATH] Responsible for constitutive and herbivore-induced simple nitrile formation. Promotes simple nitriles, but not epithionitrile or thiocyanate formation. Converts allylglucosinolate, 4-methylsulfinylbutylglucosinolate, 4-methylthiobutylglucosinolate and benzylglucosinolate to their corresponding simple nitriles in the presence of myrosinase.<ref>PMID:18987211</ref>		[https://www.uniprot.org/uniprot/JAL28_ARATH JAL28_ARATH] Responsible for constitutive and herbivore-induced simple nitrile formation. Promotes simple nitriles, but not epithionitrile or thiocyanate formation. Converts allylglucosinolate, 4-methylsulfinylbutylglucosinolate, 4-methylthiobutylglucosinolate and benzylglucosinolate to their corresponding simple nitriles in the presence of myrosinase.<ref>PMID:18987211</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	As important components of the glucosinolate-myrosinase system, specifier proteins mediate plant defense against herbivory and pathogen attacks. After tissue disruption, glucosinolates are hydrolyzed by myrosinases to instable aglucones, which will rearrange to form defensive isothiocyanates. Nevertheless, this reaction could be redirected to form other products by specifier proteins. Up to now, identified specifier proteins include epithiospecifier proteins (ESPs), thiocyanate forming proteins (TFPs), and nitrile-specifier proteins (NSPs). Recently, the structures of ESP and TFP have been reported. However, both the structure and the catalytic mechanism of NSPs remain enigmatic. Here, we solved the crystal structure of the NSP1 protein from Arabidopsis thaliana (AtNSP1). Structural comparisons with ESP and TFP proteins revealed several structural features of AtNSP1 different from those of the two proteins. Subsequent molecular docking studies showed that the R292 residue in AtNSP1 displayed a conformation different from those of the corresponding residues in ESP and TFP proteins, which might account for the product specificity and catalytic mechanism of AtNSP1. Taken together, the present study provides important insights into the molecular mechanisms underlying the different product spectrums between NSPs and the other two types of specifier proteins, and shed light on the future studies of the detailed mechanisms of other specifier proteins.
-
-	Crystal structure of the nitrile-specifier protein NSP1 from Arabidopsis thaliana.,Zhang W, Zhou Y, Wang K, Dong Y, Wang W, Feng Y Biochem Biophys Res Commun. 2017 Jun 17;488(1):147-152. doi:, 10.1016/j.bbrc.2017.05.027. Epub 2017 May 4. PMID:28479247<ref>PMID:28479247</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5gqt" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:39, 2 August 2023

OCA — Wed, 02 Aug 2023 11:39:36 GMT

←Older revision		Revision as of 11:39, 2 August 2023
Line 1:		Line 1:

	==Crystal structure of a specifier Protein from Arabidopsis thaliana==		==Crystal structure of a specifier Protein from Arabidopsis thaliana==
-	<StructureSection load='5gqt' size='340' side='right' caption='[[5gqt]], [[Resolution\|resolution]] 3.02Å' scene=''>	+	<StructureSection load='5gqt' size='340' side='right'caption='[[5gqt]], [[Resolution\|resolution]] 3.02Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5gqt]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Arath Arath~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GQT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5GQT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5gqt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GQT FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~NSP1~~, ~~JAL28, At3g16400, MDC8.2, T02O04.11 (~~[~~http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=3702 ARATH])~~</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]] 3.022Å</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=5gqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gqt OCA], [~~http~~://pdbe.org/5gqt PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5gqt RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5gqt PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5gqt 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=5gqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gqt OCA], [https://pdbe.org/5gqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gqt RCSB], [https://www.ebi.ac.uk/pdbsum/5gqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gqt ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/JAL28_ARATH JAL28_ARATH]] Responsible for constitutive and herbivore-induced simple nitrile formation. Promotes simple nitriles, but not epithionitrile or thiocyanate formation. Converts allylglucosinolate, 4-methylsulfinylbutylglucosinolate, 4-methylthiobutylglucosinolate and benzylglucosinolate to their corresponding simple nitriles in the presence of myrosinase.<ref>PMID:18987211</ref>	+	[https://www.uniprot.org/uniprot/JAL28_ARATH JAL28_ARATH] Responsible for constitutive and herbivore-induced simple nitrile formation. Promotes simple nitriles, but not epithionitrile or thiocyanate formation. Converts allylglucosinolate, 4-methylsulfinylbutylglucosinolate, 4-methylthiobutylglucosinolate and benzylglucosinolate to their corresponding simple nitriles in the presence of myrosinase.<ref>PMID:18987211</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Arath~~]]	+	[[Category: Arabidopsis thaliana]]
-	[[Category: ~~Feng, Y~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Zhang, W~~]]	+	[[Category: Feng Y]]
-	[[Category: ~~Beta propeller]]~~	+	[[Category: Zhang W]]
-	~~[[Category: Beta sheet]]~~	+
-	~~[[Category: Plant protein~~]]	+

OCA at 08:31, 16 November 2017

OCA — Thu, 16 Nov 2017 08:31:40 GMT

←Older revision		Revision as of 08:31, 16 November 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5gqt is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Crystal structure of a specifier Protein from Arabidopsis thaliana==
		+	<StructureSection load='5gqt' size='340' side='right' caption='[[5gqt]], [[Resolution\|resolution]] 3.02Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5gqt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GQT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GQT FirstGlance]. <br>
		+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NSP1, JAL28, At3g16400, MDC8.2, T02O04.11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=5gqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gqt OCA], [http://pdbe.org/5gqt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gqt RCSB], [http://www.ebi.ac.uk/pdbsum/5gqt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gqt ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/JAL28_ARATH JAL28_ARATH]] Responsible for constitutive and herbivore-induced simple nitrile formation. Promotes simple nitriles, but not epithionitrile or thiocyanate formation. Converts allylglucosinolate, 4-methylsulfinylbutylglucosinolate, 4-methylthiobutylglucosinolate and benzylglucosinolate to their corresponding simple nitriles in the presence of myrosinase.<ref>PMID:18987211</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	As important components of the glucosinolate-myrosinase system, specifier proteins mediate plant defense against herbivory and pathogen attacks. After tissue disruption, glucosinolates are hydrolyzed by myrosinases to instable aglucones, which will rearrange to form defensive isothiocyanates. Nevertheless, this reaction could be redirected to form other products by specifier proteins. Up to now, identified specifier proteins include epithiospecifier proteins (ESPs), thiocyanate forming proteins (TFPs), and nitrile-specifier proteins (NSPs). Recently, the structures of ESP and TFP have been reported. However, both the structure and the catalytic mechanism of NSPs remain enigmatic. Here, we solved the crystal structure of the NSP1 protein from Arabidopsis thaliana (AtNSP1). Structural comparisons with ESP and TFP proteins revealed several structural features of AtNSP1 different from those of the two proteins. Subsequent molecular docking studies showed that the R292 residue in AtNSP1 displayed a conformation different from those of the corresponding residues in ESP and TFP proteins, which might account for the product specificity and catalytic mechanism of AtNSP1. Taken together, the present study provides important insights into the molecular mechanisms underlying the different product spectrums between NSPs and the other two types of specifier proteins, and shed light on the future studies of the detailed mechanisms of other specifier proteins.

-	~~Authors~~:	+	Crystal structure of the nitrile-specifier protein NSP1 from Arabidopsis thaliana.,Zhang W, Zhou Y, Wang K, Dong Y, Wang W, Feng Y Biochem Biophys Res Commun. 2017 Jun 17;488(1):147-152. doi:, 10.1016/j.bbrc.2017.05.027. Epub 2017 May 4. PMID:28479247<ref>PMID:28479247</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5gqt" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Arath]]
		+	[[Category: Feng, Y]]
		+	[[Category: Zhang, W]]
		+	[[Category: Beta propeller]]
		+	[[Category: Beta sheet]]
		+	[[Category: Plant protein]]

OCA: Protected "5gqt" [edit=sysop:move=sysop]

OCA — Fri, 09 Sep 2016 11:57:13 GMT

Protected "5gqt" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:57, 9 September 2016

OCA: New page: '''Unreleased structure''' The entry 5gqt is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

OCA — Fri, 09 Sep 2016 11:57:11 GMT

New page: '''Unreleased structure''' The entry 5gqt is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5gqt is ON HOLD until Paper Publication

Authors:

Description:
[[Category: Unreleased Structures]]