1jcu: Difference between revisions
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<StructureSection load='1jcu' size='340' side='right'caption='[[1jcu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1jcu' size='340' side='right'caption='[[1jcu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jcu]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1jcu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"methanobacterium_thermoautotrophicus"_(sic)_zeikus_and_wolfe_1972 "methanobacterium thermoautotrophicus" (sic) zeikus and wolfe 1972]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JCU FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=1jcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jcu OCA], [https://pdbe.org/1jcu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jcu RCSB], [https://www.ebi.ac.uk/pdbsum/1jcu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jcu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == |
Revision as of 10:18, 14 April 2021
Solution Structure of MTH1692 Protein from Methanobacterium thermoautotrophicumSolution Structure of MTH1692 Protein from Methanobacterium thermoautotrophicum
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 PubMedThe influx of genomic sequence information has led to the concept of structural proteomics, the determination of protein structures on a genome-wide scale. Here we describe an approach to structural proteomics of small proteins using NMR spectroscopy. Over 500 small proteins from several organisms were cloned, expressed, purified, and evaluated by NMR. Although there was variability among proteomes, overall 20% of these proteins were found to be readily amenable to NMR structure determination. NMR sample preparation was centralized in one facility, and a distributive approach was used for NMR data collection and analysis. Twelve structures are reported here as part of this approach, which allowed us to infer putative functions for several conserved hypothetical proteins. An NMR approach to structural proteomics.,Yee A, Chang X, Pineda-Lucena A, Wu B, Semesi A, Le B, Ramelot T, Lee GM, Bhattacharyya S, Gutierrez P, Denisov A, Lee CH, Cort JR, Kozlov G, Liao J, Finak G, Chen L, Wishart D, Lee W, McIntosh LP, Gehring K, Kennedy MA, Edwards AM, Arrowsmith CH Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1825-30. PMID:11854485[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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