1hxv

From Proteopedia

(Difference between revisions)

Current revision

PPIASE DOMAIN OF THE MYCOPLASMA GENITALIUM TRIGGER FACTOR

Structural highlights

1hxv is a 1 chain structure with sequence from Mycoplasma genitalium. 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

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).

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

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^[1]

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

References

↑ Vogtherr M, Jacobs DM, Parac TN, Maurer M, Pahl A, Saxena K, Ruterjans H, Griesinger C, Fiebig KM. 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. J Mol Biol. 2002 May 10;318(4):1097-115. PMID:12054805 doi:10.1016/S0022-2836(02)00112-2

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==PPIASE DOMAIN OF THE MYCOPLASMA GENITALIUM TRIGGER FACTOR==
-<StructureSection load='1hxv' size='340' side='right' caption='[[1hxv]], [[NMR_Ensembles_of_Models | 12 NMR models]]' scene=''>
+<StructureSection load='1hxv' size='340' side='right'caption='[[1hxv]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hxv]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HXV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hxv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycoplasma_genitalium Mycoplasma genitalium]. 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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hxv OCA], [http://pdbe.org/1hxv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hxv RCSB], [http://www.ebi.ac.uk/pdbsum/1hxv PDBsum]</span></td></tr>
+</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=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>
 </table>
 == Function ==
-[[http://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).
+[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).
 == 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/hx/1hxv_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hx/1hxv_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1hxv ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 30: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 33530]]
+[[Category: Large Structures]]
-[[Category: Fiebig, K]]
+[[Category: Mycoplasma genitalium]]
-[[Category: Maurer, M]]
+[[Category: Fiebig K]]
-[[Category: Pahl, A]]
+[[Category: Maurer M]]
-[[Category: Parac, T N]]
+[[Category: Pahl A]]
-[[Category: Vogtherr, M]]
+[[Category: Parac TN]]
-[[Category: Chaperone]]
+[[Category: Vogtherr M]]
-[[Category: Fkbp fold]]
-[[Category: Ppiase]]

1hxv

From Proteopedia

Current revision

PPIASE DOMAIN OF THE MYCOPLASMA GENITALIUM TRIGGER FACTOR

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox