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2ith

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[[Image:2ith.jpg|left|200px]]
 
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{{Structure
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==NMR Structure of Haloferax volcanii DHFR==
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|PDB= 2ith |SIZE=350|CAPTION= <scene name='initialview01'>2ith</scene>
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<StructureSection load='2ith' size='340' side='right'caption='[[2ith]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2ith]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloferax_volcanii Haloferax volcanii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ITH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ITH FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= folA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2246 Haloferax volcanii])
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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=2ith FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ith OCA], [https://pdbe.org/2ith PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ith RCSB], [https://www.ebi.ac.uk/pdbsum/2ith PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ith ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ith FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ith OCA], [http://www.ebi.ac.uk/pdbsum/2ith PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ith RCSB]</span>
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[https://www.uniprot.org/uniprot/DYRA_HALVD DYRA_HALVD] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.<ref>PMID:2509470</ref>
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}}
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== Evolutionary Conservation ==
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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/it/2ith_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2ith ConSurf].
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<div style="clear:both"></div>
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'''NMR Structure of Haloferax volcanii DHFR'''
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==See Also==
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*[[Dihydrofolate reductase 3D structures|Dihydrofolate reductase 3D structures]]
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== References ==
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==Overview==
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<references/>
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Proteins from halophiles have adapted to challenging environmental conditions and require salt for their structure and function. How halophilic proteins adapted to a hypersaline environment is still an intriguing question. It is important to mimic the physiological conditions of the archae extreme halophiles when characterizing their enzymes, including structural characterization. The NMR derived structure of Haloferax volcanii dihydrofolate reductase in 3.5 M NaCl is presented, and represents the first high salt structure calculated using NMR data. Structure calculations show that this protein has a solution structure which is similar to the previously determined crystal structure with a difference at the N terminus of beta3 and the type of beta-turn connection beta7 and beta8.
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__TOC__
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</StructureSection>
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==About this Structure==
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2ITH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Haloferax_volcanii Haloferax volcanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ITH OCA].
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==Reference==
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Structure in an extreme environment: NMR at high salt., Binbuga B, Boroujerdi AF, Young JK, Protein Sci. 2007 Aug;16(8):1783-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17656587 17656587]
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[[Category: Dihydrofolate reductase]]
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[[Category: Haloferax volcanii]]
[[Category: Haloferax volcanii]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Binbuga, B.]]
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[[Category: Binbuga B]]
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[[Category: dhfr]]
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[[Category: dihydrofolate reductase]]
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[[Category: halophilic archaea]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:48:28 2008''
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Current revision

NMR Structure of Haloferax volcanii DHFR

PDB ID 2ith

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