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==Crystal Structure of the Electron Transfer Flavoprotein Subunit Alpha related Protein Ta0212 from Thermoplasma acidophilum== | |||
<StructureSection load='3fet' size='340' side='right'caption='[[3fet]], [[Resolution|resolution]] 2.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3fet]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FET 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]] 2.05Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=3fet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fet OCA], [https://pdbe.org/3fet PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fet RCSB], [https://www.ebi.ac.uk/pdbsum/3fet PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fet ProSAT], [https://www.topsan.org/Proteins/MCSG/3fet TOPSAN]</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/fe/3fet_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3fet ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacillus anthracisproduces metabolically inactive spores. Germination of these spores requires germination-specific lytic enzymes (GSLEs) that degrade the unique cortex peptidoglycan to permit resumption of metabolic activity and outgrowth. We report the first crystal structure of the catalytic domain of a GSLE, SleB. The structure revealed a transglycosylase fold with unique active site topology and permitted identification of the catalytic glutamate residue. Moreover, the structure provided insights into the molecular basis for the specificity of the enzyme for muramic-delta-lactam-containing cortex peptidoglycan. The protein also contains a metal-binding site that is positioned directly at the entrance of the substrate-binding cleft. Proteins 2012. (c) 2012 Wiley Periodicals, Inc. | |||
The catalytic domain of the germination-specific lytic transglycosylasesleb from bacillus anthracisdisplays a unique active site topology.,Jing X, Robinson HR, Heffron J, Popham DL, Schubot FD Proteins. 2012 Jul 7. doi: 10.1002/prot.24140. PMID:022777830<ref>PMID:022777830</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3fet" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Thermoplasma acidophilum]] | [[Category: Thermoplasma acidophilum]] | ||
[[Category: Joachimiak | [[Category: Joachimiak A]] | ||
[[Category: Kim | [[Category: Kim Y]] | ||
[[Category: Moy S]] | |||
[[Category: Moy | [[Category: Souvong K]] | ||
[[Category: Souvong | [[Category: Tesar C]] | ||
[[Category: Tesar | |||
Latest revision as of 09:13, 27 November 2024
Structural highlights
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 PubMedBacillus anthracisproduces metabolically inactive spores. Germination of these spores requires germination-specific lytic enzymes (GSLEs) that degrade the unique cortex peptidoglycan to permit resumption of metabolic activity and outgrowth. We report the first crystal structure of the catalytic domain of a GSLE, SleB. The structure revealed a transglycosylase fold with unique active site topology and permitted identification of the catalytic glutamate residue. Moreover, the structure provided insights into the molecular basis for the specificity of the enzyme for muramic-delta-lactam-containing cortex peptidoglycan. The protein also contains a metal-binding site that is positioned directly at the entrance of the substrate-binding cleft. Proteins 2012. (c) 2012 Wiley Periodicals, Inc. The catalytic domain of the germination-specific lytic transglycosylasesleb from bacillus anthracisdisplays a unique active site topology.,Jing X, Robinson HR, Heffron J, Popham DL, Schubot FD Proteins. 2012 Jul 7. doi: 10.1002/prot.24140. PMID:022777830[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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