2rih

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[[Image:2rih.jpg|left|200px]]
 
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==CBS domain protein PAE2072 from Pyrobaculum aerophilum==
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The line below this paragraph, containing "STRUCTURE_2rih", creates the "Structure Box" on the page.
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<StructureSection load='2rih' size='340' side='right'caption='[[2rih]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<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>
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{{STRUCTURE_2rih| PDB=2rih | SCENE= }}
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<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>
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</table>
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'''CBS domain protein PAE2072 from Pyrobaculum aerophilum'''
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== Function ==
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[https://www.uniprot.org/uniprot/Q8ZVX8_PYRAE Q8ZVX8_PYRAE]
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ri/2rih_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== 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.
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.
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==About this Structure==
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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>
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2RIH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RIH OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/18513746 18513746]
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</div>
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[[Category: Pyrobaculum aerophilum]]
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<div class="pdbe-citations 2rih" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Cascio, D.]]
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<references/>
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[[Category: King, N P.]]
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__TOC__
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[[Category: Lee, T M.]]
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</StructureSection>
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[[Category: Sawaya, M R.]]
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[[Category: Large Structures]]
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[[Category: Yeates, T O.]]
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[[Category: Pyrobaculum aerophilum str. IM2]]
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[[Category: Amp binding protein]]
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[[Category: Cascio D]]
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[[Category: Bateman domain]]
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[[Category: King NP]]
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[[Category: Cbs domain]]
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[[Category: Lee TM]]
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[[Category: Ligand-binding protein]]
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[[Category: Sawaya MR]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:04:18 2008''
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[[Category: Yeates TO]]

Current revision

CBS domain protein PAE2072 from Pyrobaculum aerophilum

PDB ID 2rih

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