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==NMR Structure of Haloferax volcanii DHFR==
==NMR Structure of Haloferax volcanii DHFR==
<StructureSection load='2ith' size='340' side='right'caption='[[2ith]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2ith' size='340' side='right'caption='[[2ith]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ith]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_29605 Atcc 29605]. 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>
<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>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">folA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2246 ATCC 29605])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </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=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>
<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>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/DYR_HALVD DYR_HALVD]] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).  
[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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
Structure in an extreme environment: NMR at high salt.,Binbuga B, Boroujerdi AF, Young JK Protein Sci. 2007 Aug;16(8):1783-7. PMID:17656587<ref>PMID:17656587</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ith" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 29605]]
[[Category: Haloferax volcanii]]
[[Category: Dihydrofolate reductase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Binbuga, B]]
[[Category: Binbuga B]]
[[Category: Dhfr]]
[[Category: Halophilic archaea]]
[[Category: Oxidoreductase]]

Latest revision as of 09:41, 1 May 2024

NMR Structure of Haloferax volcanii DHFRNMR Structure of Haloferax volcanii DHFR

Structural highlights

2ith is a 1 chain structure with sequence from Haloferax volcanii. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DYRA_HALVD Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Zusman T, Rosenshine I, Boehm G, Jaenicke R, Leskiw B, Mevarech M. Dihydrofolate reductase of the extremely halophilic archaebacterium Halobacterium volcanii. The enzyme and its coding gene. J Biol Chem. 1989 Nov 15;264(32):18878-83 PMID:2509470
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