1ix5

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[[Image:1ix5.png|left|200px]]
 
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==Solution structure of the Methanococcus thermolithotrophicus FKBP==
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The line below this paragraph, containing "STRUCTURE_1ix5", creates the "Structure Box" on the page.
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<StructureSection load='1ix5' size='340' side='right'caption='[[1ix5]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ix5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermococcus_thermolithotrophicus Methanothermococcus thermolithotrophicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IX5 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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'>[https://proteopedia.org/fgij/fg.htm?mol=1ix5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ix5 OCA], [https://pdbe.org/1ix5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ix5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ix5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ix5 ProSAT]</span></td></tr>
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{{STRUCTURE_1ix5| PDB=1ix5 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FKBPS_METTL FKBPS_METTL] Catalyzes the cis-trans isomerization of peptidyl prolyl bonds and accelerates protein folding (PubMed:9440528, PubMed:10631007). Also exhibits chaperone-like activity (PubMed:10631007). In vitro, can use oligopeptides such as N-succinyl-Ala-Leu-Pro-Phe-p-nitroanilide and N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide as substrates (PubMed:9440528, PubMed:10631007).<ref>PMID:10631007</ref> <ref>PMID:9440528</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ix/1ix5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1ix5 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Here we report the solution structure of an archaeal FK506-binding protein (FKBP) from a thermophilic archaeum, Methanococcus thermolithotrophicus (MtFKBP17), which has peptidyl prolyl cis-trans isomerase (PPIase) and chaperone-like activities, to reveal the structural basis for the dual function. In addition to a typical PPIase domain, a newly identified domain is formed in the flap loop by a 48-residue insert that is required for the chaperone-like activity. The new domain, called IF domain (the Insert in the Flap), is a novel-folding motif and exposes a hydrophobic surface, which we consider to play an important role in the chaperone-like activity.
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===Solution structure of the Methanococcus thermolithotrophicus FKBP===
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Three-dimensional solution structure of an archaeal FKBP with a dual function of peptidyl prolyl cis-trans isomerase and chaperone-like activities.,Suzuki R, Nagata K, Yumoto F, Kawakami M, Nemoto N, Furutani M, Adachi K, Maruyama T, Tanokura M J Mol Biol. 2003 May 16;328(5):1149-60. PMID:12729748<ref>PMID:12729748</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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The line below this paragraph, {{ABSTRACT_PUBMED_12729748}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1ix5" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12729748 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12729748}}
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==About this Structure==
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[[1ix5]] is a 1 chain structure of [[Cyclophilin]] with sequence from [http://en.wikipedia.org/wiki/Methanothermococcus_thermolithotrophicus Methanothermococcus thermolithotrophicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IX5 OCA].
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==See Also==
==See Also==
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*[[Cyclophilin]]
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*[[FKBP 3D structures|FKBP 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:12729748</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Methanothermococcus thermolithotrophicus]]
[[Category: Methanothermococcus thermolithotrophicus]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Adachi K]]
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[[Category: Adachi, K.]]
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[[Category: Furutani M]]
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[[Category: Furutani, M.]]
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[[Category: Kawakami M]]
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[[Category: Kawakami, M.]]
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[[Category: Maruyama T]]
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[[Category: Maruyama, T.]]
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[[Category: Nagata K]]
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[[Category: Nagata, K.]]
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[[Category: Nemoto N]]
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[[Category: Nemoto, N.]]
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[[Category: Suzuki R]]
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[[Category: Suzuki, R.]]
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[[Category: Tanokura M]]
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[[Category: Tanokura, M.]]
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[[Category: Fkbp fold]]
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[[Category: Isomerase]]
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[[Category: Ppiase]]
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Current revision

Solution structure of the Methanococcus thermolithotrophicus FKBP

PDB ID 1ix5

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OCA

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