2rih
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2rih is ON HOLD until Paper Publication Authors: Lee, T.M., King, N.P., Sawaya, M.R., Cascio, D., Yeates, T.O. Description: CBS domain protein PAE2...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==CBS domain protein PAE2072 from Pyrobaculum aerophilum== | |
| + | <StructureSection load='2rih' size='340' side='right'caption='[[2rih]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2rih]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_aerophilum_str._IM2 Pyrobaculum aerophilum str. IM2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RIH 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]] 2.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2rih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rih OCA], [https://pdbe.org/2rih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rih RCSB], [https://www.ebi.ac.uk/pdbsum/2rih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rih ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q8ZVX8_PYRAE Q8ZVX8_PYRAE] | ||
| + | == 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/ri/2rih_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=2rih ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cystathionine beta-synthase domains are found in a myriad of proteins from organisms across the tree of life and have been hypothesized to function as regulatory modules that sense the energy charge of cells. Here we characterize the structure and stability of PAE2072, a dimeric tandem cystathionine beta-synthase domain protein from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum. Crystal structures of the protein in unliganded and AMP-bound forms, determined at resolutions of 2.10 and 2.35 A, respectively, reveal remarkable conservation of key functional features seen in the gamma subunit of the eukaryotic AMP-activated protein kinase. The structures also confirm the presence of a suspected intermolecular disulfide bond between the two subunits that is shown to stabilize the protein. Our AMP-bound structure represents a first step in investigating the function of a large class of uncharacterized prokaryotic proteins. In addition, this work extends previous studies that have suggested that, in certain thermophilic microbes, disulfide bonds play a key role in stabilizing intracellular proteins and protein-protein complexes. | ||
| - | + | Structures and functional implications of an AMP-binding cystathionine beta-synthase domain protein from a hyperthermophilic archaeon.,King NP, Lee TM, Sawaya MR, Cascio D, Yeates TO J Mol Biol. 2008 Jun 27;380(1):181-92. Epub 2008 May 7. PMID:18513746<ref>PMID:18513746</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2rih" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pyrobaculum aerophilum str. IM2]] | ||
| + | [[Category: Cascio D]] | ||
| + | [[Category: King NP]] | ||
| + | [[Category: Lee TM]] | ||
| + | [[Category: Sawaya MR]] | ||
| + | [[Category: Yeates TO]] | ||
Current revision
CBS domain protein PAE2072 from Pyrobaculum aerophilum
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