1ix5

From Proteopedia

(Difference between revisions)

Revision as of 11:07, 4 August 2021

Solution structure of the Methanococcus thermolithotrophicus FKBP

Structural highlights

1ix5 is a 1 chain structure with sequence from Atcc 35097. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Peptidylprolyl isomerase, with EC number 5.2.1.8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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^[1]

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

References

↑ 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

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ix5"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ix5' size='340' side='right'caption='[[1ix5]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ix5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35097 Atcc 35097]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IX5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ix5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35097 Atcc 35097]. 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>
-</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>
+</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
-<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=1ix5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ix5 OCA], [http://pdbe.org/1ix5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ix5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ix5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ix5 ProSAT]</span></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=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>
 == Evolutionary Conservation ==
@@ Line 28: / Line 28: @@
 ==See Also==
-*[[FK506 binding protein|FK506 binding protein]]
+*[[FKBP 3D structures|FKBP 3D structures]]
 == References ==
 <references/>

1ix5

From Proteopedia

Revision as of 11:07, 4 August 2021

Solution structure of the Methanococcus thermolithotrophicus FKBP

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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