1ryk
From Proteopedia
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| - | [[Image:1ryk.gif|left|200px]]<br /><applet load="1ryk" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1ryk" /> | ||
| - | '''Solution NMR Structure Protein yjbJ from Escherichia coli. Northeast Structural Genomics Consortium Target ET93; Ontario Centre for Structural Proteomics target EC0298_1_69;'''<br /> | ||
| - | == | + | ==Solution NMR Structure Protein yjbJ from Escherichia coli. Northeast Structural Genomics Consortium Target ET93; Ontario Centre for Structural Proteomics target EC0298_1_69;== |
| + | <StructureSection load='1ryk' size='340' side='right'caption='[[1ryk]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1ryk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1jyg 1jyg]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RYK FirstGlance]. <br> | ||
| + | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ryk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ryk OCA], [https://pdbe.org/1ryk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ryk RCSB], [https://www.ebi.ac.uk/pdbsum/1ryk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ryk ProSAT], [https://www.topsan.org/Proteins/NESGC/1ryk TOPSAN]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/YJBJ_ECOLI YJBJ_ECOLI] | ||
| + | == 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/ry/1ryk_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1ryk ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The 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. | The 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<ref>PMID:11854485</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1ryk" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Arrowsmith | + | [[Category: Arrowsmith CH]] |
| - | [[Category: Cort | + | [[Category: Cort JR]] |
| - | [[Category: Edwards | + | [[Category: Edwards AM]] |
| - | [[Category: Kennedy | + | [[Category: Kennedy MA]] |
| - | [[Category: Liao | + | [[Category: Liao J]] |
| - | + | [[Category: Pineda-Lucena A]] | |
| - | [[Category: Pineda-Lucena | + | [[Category: Wu B]] |
| - | [[Category: Wu | + | [[Category: Yee A]] |
| - | [[Category: Yee | + | |
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Current revision
Solution NMR Structure Protein yjbJ from Escherichia coli. Northeast Structural Genomics Consortium Target ET93; Ontario Centre for Structural Proteomics target EC0298_1_69;
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Categories: Escherichia coli | Large Structures | Arrowsmith CH | Cort JR | Edwards AM | Kennedy MA | Liao J | Pineda-Lucena A | Wu B | Yee A
