2uz5: Difference between revisions
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< | ==Solution structure of the fkbp-domain of Legionella pneumophila Mip== | ||
<StructureSection load='2uz5' size='340' side='right'caption='[[2uz5]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2uz5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UZ5 FirstGlance]. <br> | |||
</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'>[https://proteopedia.org/fgij/fg.htm?mol=2uz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uz5 OCA], [https://pdbe.org/2uz5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uz5 RCSB], [https://www.ebi.ac.uk/pdbsum/2uz5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uz5 ProSAT]</span></td></tr> | |||
</table> | |||
== 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/uz/2uz5_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=2uz5 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The homodimeric 45.6 kDa (total mass) Mip protein, a virulence factor from Legionella pneumophila, was investigated with solution NMR spectroscopy and molecular dynamics (MD) simulations. Two Mip monomers are dimerized via an N-terminal helix bundle that is connected via a long alpha-helix to a C-terminal FKBP domain in each subunit. More than 85% of the amino acids were identified in triple-resonance NMR spectra. (15)N relaxation analysis showed a bimodal distribution of R(1)/R(2) values, with the lower ratio in the N-terminal domain. Relaxation dispersion measurements confirmed that these reduced ratios did not originate from conformational exchange. Thus, two different correlation times (tau(c)) can be deduced, reflecting partly uncoupled motions of both domains. Relaxation data of a Mip(77)(-)(213) monomer mutant were similar to those observed in the dimer, corroborating that the FKBP domain, including part of the connecting helix, behaves as one dynamic entity. MD simulations (18 ns) of the Mip dimer also yielded two different correlation times for the two domains and thus confirm the independence of the domain motions. Principal component analysis of the dihedral space covariance matrix calculated from the MD trajectory suggests a flexible region in the long connecting helix that acts as a hinge between the two domains. Such motion provides a possible explanation of how Mip can bind to complex molecular components of the extracellular matrix and mediate alveolar damage and bacterial spread in the lung. | |||
Domain motions of the Mip protein from Legionella pneumophila.,Horstmann M, Ehses P, Schweimer K, Steinert M, Kamphausen T, Fischer G, Hacker J, Rosch P, Faber C Biochemistry. 2006 Oct 10;45(40):12303-11. PMID:17014083<ref>PMID:17014083</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2uz5" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Legionella pneumophila]] | [[Category: Legionella pneumophila]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Ceymann, A]] | |||
[[Category: Ceymann, A | [[Category: Ehses, P]] | ||
[[Category: Ehses, P | [[Category: Faber, C]] | ||
[[Category: Faber, C | [[Category: Fischer, G]] | ||
[[Category: Fischer, G | [[Category: Hacker, J]] | ||
[[Category: Hacker, J | [[Category: Horstmann, M]] | ||
[[Category: Horstmann, M | [[Category: Kamphausen, T]] | ||
[[Category: Kamphausen, T | [[Category: Rosch, P]] | ||
[[Category: Rosch, P | [[Category: Schweimer, K]] | ||
[[Category: Schweimer, K | [[Category: Steinert, M]] | ||
[[Category: Steinert, M | |||
[[Category: Fkbp]] | [[Category: Fkbp]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Legionnaires disease]] | [[Category: Legionnaires disease]] | ||
[[Category: Ppiase]] | [[Category: Ppiase]] | ||