1hxv

<StructureSection load='1hxv' size='340' side='right'caption='[[1hxv]], [[NMR_Ensembles_of_Models | 12 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1hxv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_33530 Atcc 33530]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HXV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HXV FirstGlance]. <br>

</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=1hxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hxv OCA], [https://pdbe.org/1hxv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hxv RCSB], [https://www.ebi.ac.uk/pdbsum/1hxv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hxv ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/TIG_MYCGE TIG_MYCGE]] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).

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== Publication Abstract from PubMed ==

We have solved the solution structure of the peptidyl-prolyl cis-trans isomerase (PPIase) domain of the trigger factor from Mycoplasma genitalium by homo- and heteronuclear NMR spectroscopy. Our results lead to a well-defined structure with a backbone rmsd of 0.23 A. As predicted, the PPIase domain of the trigger factor adopts the FK506 binding protein (FKBP) fold. Furthermore, our NMR relaxation data indicate that the dynamic behavior of the trigger factor PPIase domain and of FKBP are similar. Structural variations when compared to FKBP exist in the flap region and within the bulges of strand 5 of the beta sheet. Although the active-site crevice is similar to that of FKBP, subtle steric variations in this region can explain why FK506 does not bind to the trigger factor. Sequence variability (27% identity) between trigger factor and FKBP results in significant differences in surface charge distribution and the absence of the first strand of the central beta sheet. Our data indicate, however, that this strand may be partially structured as "nascent" beta strand. This makes the trigger factor PPIase domain the most minimal representative of the FKBP like protein family of PPIases.

NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein.,Vogtherr M, Jacobs DM, Parac TN, Maurer M, Pahl A, Saxena K, Ruterjans H, Griesinger C, Fiebig KM J Mol Biol. 2002 May 10;318(4):1097-115. PMID:12054805<ref>PMID:12054805</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1hxv" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 33530]]

[[Category: Fiebig, K]]

[[Category: Maurer, M]]

[[Category: Pahl, A]]

[[Category: Parac, T N]]

[[Category: Vogtherr, M]]

[[Category: Ppiase]]