View source for 7dek


==Pseudomonas aeruginosa FK506-binding protein PaFkbA==
<StructureSection load='7dek' size='340' side='right'caption='[[7dek]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7dek]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DEK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</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=7dek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dek OCA], [https://pdbe.org/7dek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dek RCSB], [https://www.ebi.ac.uk/pdbsum/7dek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dek ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9HYX8_PSEAE Q9HYX8_PSEAE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial Mip-like FK506-binding proteins (FKBPs) mostly exhibit peptidyl-prolyl-cis/trans-isomerase (PPIase) and chaperone activities. These activities are associated with various intracellular functions with diverse molecular mechanisms. Herein, we report the PA3262 gene-encoded crystal structure of the Pseudomonas aeruginosa PAO1's Mip-like protein PaFkbA. Biochemical characterization of PaFkbA demonstrated PaFkbA's chaperone activity for periplasmic protein MucD, a negative regulator of alginate biosynthesis. Furthermore, structural analysis of PaFkbA was used to describe the key features of PaFkbA chaperone activity. The outcomes of this analysis showed that the hinge region in the connecting helix of PaFbkA leads to the crucial conformational state transition for PaFkbA activity. Besides, the N-terminal domains participated in dimerization, and revealed its potential connection with FKBP domain and substrate binding. Mutagenesis and chaperone activity assay supported the theory that inter-domain motions are essential for PaFkbA function. These results provide biochemical and structural insights into the mechanism for FKBP's chaperone activity and establish a plausible correlation between PaFkbA and P. aeruginosa MucD.

Structural characterization of PaFkbA: A periplasmic chaperone from Pseudomonas aeruginosa.,Huang Q, Yang J, Li C, Song Y, Zhu Y, Zhao N, Mou X, Tang X, Luo G, Tong A, Sun B, Tang H, Li H, Bai L, Bao R Comput Struct Biotechnol J. 2021 Apr 25;19:2460-2467. doi:, 10.1016/j.csbj.2021.04.045. eCollection 2021. PMID:34025936<ref>PMID:34025936</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7dek" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Bao R]]
[[Category: Huang Q]]
[[Category: Ynag J]]