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[[Image:1ix5.jpg|left|200px]]


{{Structure
==Solution structure of the Methanococcus thermolithotrophicus FKBP==
|PDB= 1ix5 |SIZE=350|CAPTION= <scene name='initialview01'>1ix5</scene>
<StructureSection load='1ix5' size='340' side='right'caption='[[1ix5]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<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>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE=  
<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>
}}
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ix/1ix5_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


'''Solution structure of the Methanococcus thermolithotrophicus FKBP'''
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ix5" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[FKBP 3D structures|FKBP 3D structures]]
 
== References ==
==About this Structure==
<references/>
1IX5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermococcus_thermolithotrophicus Methanothermococcus thermolithotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IX5 OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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:[http://www.ncbi.nlm.nih.gov/pubmed/12729748 12729748]
[[Category: Methanothermococcus thermolithotrophicus]]
[[Category: Methanothermococcus thermolithotrophicus]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Adachi K]]
[[Category: Single protein]]
[[Category: Furutani M]]
[[Category: Adachi, K.]]
[[Category: Kawakami M]]
[[Category: Furutani, M.]]
[[Category: Maruyama T]]
[[Category: Kawakami, M.]]
[[Category: Nagata K]]
[[Category: Maruyama, T.]]
[[Category: Nemoto N]]
[[Category: Nagata, K.]]
[[Category: Suzuki R]]
[[Category: Nemoto, N.]]
[[Category: Tanokura M]]
[[Category: Suzuki, R.]]
[[Category: Tanokura, M.]]
[[Category: fkbp fold]]
[[Category: ppiase]]
 
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Latest revision as of 23:38, 27 December 2023

Solution structure of the Methanococcus thermolithotrophicus FKBP

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