1ix5: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(15 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[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]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:56:07 2008''

Latest revision as of 02:38, 28 December 2023

Solution structure of the Methanococcus thermolithotrophicus FKBPSolution structure of the Methanococcus thermolithotrophicus FKBP

Structural highlights

1ix5 is a 1 chain structure with sequence from Methanothermococcus thermolithotrophicus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Furutani M, Ideno A, Iida T, Maruyama T. FK506 binding protein from a thermophilic archaeon, Methanococcus thermolithotrophicus, has chaperone-like activity in vitro. Biochemistry. 2000 Jan 18;39(2):453-62. PMID:10631007 doi:10.1021/bi9911076
  2. ↑ Furutani M, Iida T, Yamano S, Kamino K, Maruyama T. Biochemical and genetic characterization of an FK506-sensitive peptidyl prolyl cis-trans isomerase from a thermophilic archaeon, Methanococcus thermolithotrophicus. J Bacteriol. 1998 Jan;180(2):388-94. PMID:9440528 doi:10.1128/JB.180.2.388-394.1998
  3. ↑ Suzuki R, Nagata K, Yumoto F, Kawakami M, Nemoto N, Furutani M, Adachi K, Maruyama T, Tanokura M. Three-dimensional solution structure of an archaeal FKBP with a dual function of peptidyl prolyl cis-trans isomerase and chaperone-like activities. J Mol Biol. 2003 May 16;328(5):1149-60. PMID:12729748
Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1ix5&oldid=4005955"