OCA at 12:58, 1 February 2024

2024-02-01T12:58:04Z

←Older revision		Revision as of 12:58, 1 February 2024
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-	====	+	==ttSlyD FKBP domain with M8A pseudo-wild-type S2 peptide==
-	<StructureSection load='7oxg' size='340' side='right'caption='[[7oxg]]' scene=''>	+	<StructureSection load='7oxg' size='340' side='right'caption='[[7oxg]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7oxg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OXG FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7oxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oxg OCA], [https://pdbe.org/7oxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oxg RCSB], [https://www.ebi.ac.uk/pdbsum/7oxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oxg ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</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=7oxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oxg OCA], [https://pdbe.org/7oxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oxg RCSB], [https://www.ebi.ac.uk/pdbsum/7oxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oxg ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/Q5SLE7_THET8 Q5SLE7_THET8]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Peptidyl-prolyl isomerases (PPIases) catalyze intrinsically slow and often rate-limiting isomerization of prolyl-peptide bonds in unfolded or partially folded proteins, thereby speeding up the folding process and preventing misfolding. They often possess binding and chaperone domains in addition to the domain carrying the isomerization activity. Although generally, their substrates display no identity in their amino acid sequence upstream and downstream of the proline with 20 possibilities for each residue, PPIases are efficient enzymes. SlyD is a highly efficient PPIase consisting of an isomerase domain and an additional chaperone domain. The binding of peptide substrates to SlyD and its enzymatic activity depend to some extend on the proline-proximal residues, however, the impact of proline-distant residues has not been investigated so far. Here, we introduce a label-free NMR-based method to measure SlyD activity on different peptide substrates and analysed the data in the context of obtained binding affinities and several co-crystal structures. We show that especially charged and aromatic residues up to eight positions downstream and three positions upstream of the proline and outside the canonical region of similar conformations affect the activity and binding, although they rarely display distinct conformations in our crystal structures. We hypothesize that these positions primarily influence the association reaction. In the absence of the chaperone domain the isomerase activity strongly correlates with substrate affinity, whereas additional factors play a role in its presence. The mutual orientation of isomerase and chaperone domains depends on the presence of substrates in both binding sites, implying allosteric regulation of enzymatic activity.
		+
		+	Impact of distant peptide substrate residues on enzymatic activity of SlyD.,Pazicky S, Werle AA, Lei J, Low C, Weininger U Cell Mol Life Sci. 2022 Feb 19;79(3):138. doi: 10.1007/s00018-022-04179-4. PMID:35184231<ref>PMID:35184231</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7oxg" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Peptidyl-prolyl cis-trans isomerase 3D structures\|Peptidyl-prolyl cis-trans isomerase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Escherichia coli K-12]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Z-disk~~]]	+	[[Category: Thermus thermophilus HB8]]
		+	[[Category: Lei J]]
		+	[[Category: Loew C]]
		+	[[Category: Pazicky S]]

OCA at 06:14, 16 March 2022

2022-03-16T06:14:28Z

←Older revision		Revision as of 06:14, 16 March 2022
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-	'''Unreleased structure'''

-	~~The entry~~ 7oxg ~~is ON HOLD until Paper Publication~~	+	====
-		+	<StructureSection load='7oxg' size='340' side='right'caption='[[7oxg]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
-	~~Description~~:	+	</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=7oxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oxg OCA], [https://pdbe.org/7oxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oxg RCSB], [https://www.ebi.ac.uk/pdbsum/7oxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oxg ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Z-disk]]

OCA at 07:53, 21 July 2021

2021-07-21T07:53:23Z

←Older revision		Revision as of 07:53, 21 July 2021
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7oxg is ON HOLD	+	The entry 7oxg is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "7oxg" [edit=sysop:move=sysop]

2021-07-02T02:35:45Z

Protected "7oxg" [edit=sysop:move=sysop]

←Older revision

Revision as of 02:35, 2 July 2021

OCA: New page: '''Unreleased structure''' The entry 7oxg is ON HOLD Authors: Description: Category: Unreleased Structures

2021-07-02T02:35:44Z

New page: '''Unreleased structure''' The entry 7oxg is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 7oxg is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]

7oxg - Revision history

OCA at 12:58, 1 February 2024

OCA at 06:14, 16 March 2022

OCA at 07:53, 21 July 2021

OCA: Protected "7oxg" [edit=sysop:move=sysop]

OCA: New page: '''Unreleased structure''' The entry 7oxg is ON HOLD Authors: Description: Category: Unreleased Structures