5zr0

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==Solution structure of peptidyl-prolyl cis/trans isomerase domain of Trigger Factor in complex with MBP==
==Solution structure of peptidyl-prolyl cis/trans isomerase domain of Trigger Factor in complex with MBP==
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<StructureSection load='5zr0' size='340' side='right' caption='[[5zr0]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='5zr0' size='340' side='right'caption='[[5zr0]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5zr0]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZR0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZR0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5zr0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BW2952 Escherichia coli BW2952] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZR0 FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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=5zr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zr0 OCA], [http://pdbe.org/5zr0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zr0 RCSB], [http://www.ebi.ac.uk/pdbsum/5zr0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zr0 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5zr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zr0 OCA], [https://pdbe.org/5zr0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zr0 RCSB], [https://www.ebi.ac.uk/pdbsum/5zr0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zr0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
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[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/TIG_ECOLI TIG_ECOLI] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to nascent polypeptide chains via ribosomal protein L23 (PubMed:12226666). Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity.<ref>PMID:8633085</ref> <ref>PMID:8521806</ref> <ref>PMID:14726952</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Molecular chaperones often possess functional modules that are specialized in assisting the formation of specific structural elements, such as disulfide bridges and peptidyl-prolyl bonds in the cis form, in the client protein. A ribosome-associated molecular chaperone called trigger factor (TF), which has a peptidyl-prolyl cis/trans isomerase (PPIase) domain, acts as a highly efficient catalyst in the folding process limited by peptidyl-prolyl isomerization. Herein, we report on the mechanism through which TF recognizes the proline residue in the unfolded client protein during the cis/trans isomerization process. The solution structure of TF in complex with the client protein revealed that TF recognizes proline-aromatic motif located in the hydrophobic stretch of the unfolded client protein through its conserved hydrophobic cleft, suggesting that TF preferentially accelerates the isomerization of the peptidyl-prolyl bond that is eventually folded into the core of the protein in its native fold. Molecular dynamics simulation revealed that TF exploits the backbone amide group of Ile195 to form an intermolecular hydrogen bond with the carbonyl oxygen of the amino acid residue preceding the proline residue at the transition state. This intermolecular hydrogen bond presumably stabilizes the transition state and thus accelerates the isomerization. The importance of such intermolecular hydrogen bond formation during the catalysis was further corroborated by activity assays and NMR relaxation analysis. Our results suggest that both the intermolecular hydrogen bond at the transition state and the hydrophobic environment around the peptidyl-prolyl bond in the client protein play major roles in TF-mediated proline cis/trans isomerization.
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Structural insight into proline cis/trans isomerization of unfolded proteins catalyzed by the Trigger Factor chaperone.,Kawagoe S, Nakagawa H, Kumeta H, Ishimori K, Saio T J Biol Chem. 2018 Aug 9. pii: RA118.003579. doi: 10.1074/jbc.RA118.003579. PMID:30093407<ref>PMID:30093407</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5zr0" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Escherichia coli BW2952]]
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[[Category: Ishimori, K]]
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[[Category: Escherichia coli K-12]]
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[[Category: Kawagoe, S]]
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[[Category: Large Structures]]
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[[Category: Kumeta, H]]
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[[Category: Ishimori K]]
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[[Category: Nakagawa, H]]
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[[Category: Kawagoe S]]
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[[Category: Saio, T]]
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[[Category: Kumeta H]]
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[[Category: Chaperone]]
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[[Category: Nakagawa H]]
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[[Category: Molecular chaperone]]
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[[Category: Saio T]]
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[[Category: Peptidyl-prolyl isomerase]]
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Current revision

Solution structure of peptidyl-prolyl cis/trans isomerase domain of Trigger Factor in complex with MBP

PDB ID 5zr0

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