2kfw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:45, 1 May 2024) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2kfw.png|left|200px]]
 
-
{{STRUCTURE_2kfw| PDB=2kfw | SCENE= }}
+
==Solution structure of full-length SlyD from E.coli==
-
 
+
<StructureSection load='2kfw' size='340' side='right'caption='[[2kfw]]' scene=''>
-
===Solution structure of full-length SlyD from E.coli===
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[2kfw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KFW FirstGlance]. <br>
-
{{ABSTRACT_PUBMED_19645725}}
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2kfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kfw OCA], [https://pdbe.org/2kfw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kfw RCSB], [https://www.ebi.ac.uk/pdbsum/2kfw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kfw ProSAT]</span></td></tr>
-
==About this Structure==
+
</table>
-
[[2kfw]] is a 1 chain structure of [[Cyclophilin]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KFW OCA].
+
== Function ==
 +
[https://www.uniprot.org/uniprot/SLYD_ECOLI SLYD_ECOLI] Folding helper with both chaperone and peptidyl-prolyl cis-trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa-Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in Tat-dependent translocation, by binding to the Tat-type signal of folded proteins. The PPIase substrate specificity, carried out with synthetic peptides of the 'suc-Ala-Xaa-Pro-Phe-4NA' type (where Xaa is the AA tested), was found to be Phe > Ala > Leu.<ref>PMID:12100551</ref> <ref>PMID:15569666</ref> <ref>PMID:16388577</ref> <ref>PMID:17720786</ref> <ref>PMID:17215254</ref> <ref>PMID:19356587</ref> Required for lysis of phiX174 infected cells by stabilizing the hydrophobic viral lysis protein E and allowing it to accumulate to the levels required to exert its lytic effect. May act by a chaperone-like mechanism.<ref>PMID:12100551</ref> <ref>PMID:15569666</ref> <ref>PMID:16388577</ref> <ref>PMID:17720786</ref> <ref>PMID:17215254</ref> <ref>PMID:19356587</ref> Also involved in hydrogenase metallocenter assembly, probably by participating in the nickel insertion step. This function in hydrogenase biosynthesis requires chaperone activity and the presence of the metal-binding domain, but not PPIase activity.<ref>PMID:12100551</ref> <ref>PMID:15569666</ref> <ref>PMID:16388577</ref> <ref>PMID:17720786</ref> <ref>PMID:17215254</ref> <ref>PMID:19356587</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/kf/2kfw_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=2kfw ConSurf].
 +
<div style="clear:both"></div>
==See Also==
==See Also==
-
*[[Cyclophilin|Cyclophilin]]
+
*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:019645725</ref><references group="xtra"/>
+
__TOC__
 +
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Peptidylprolyl isomerase]]
+
[[Category: Large Structures]]
-
[[Category: Conte, M R.]]
+
[[Category: Conte MR]]
-
[[Category: Giancola, C.]]
+
[[Category: Giancola C]]
-
[[Category: Hands-Taylor, K L.]]
+
[[Category: Hands-Taylor KL]]
-
[[Category: He, Y.]]
+
[[Category: He Y]]
-
[[Category: Kelly, G.]]
+
[[Category: Kelly G]]
-
[[Category: Martino, L.]]
+
[[Category: Martino L]]
-
[[Category: Valentine, E R.]]
+
[[Category: Valentine ER]]
-
[[Category: Cobalt]]
+
-
[[Category: Isomerase]]
+
-
[[Category: Metal-binding]]
+
-
[[Category: Nickel]]
+
-
[[Category: Protein]]
+
-
[[Category: Rotamase]]
+
-
[[Category: Slyd]]
+

Current revision

Solution structure of full-length SlyD from E.coli

PDB ID 2kfw

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2kfw"
Personal tools