1jrm: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 2: Line 2:
<StructureSection load='1jrm' size='340' side='right' caption='[[1jrm]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
<StructureSection load='1jrm' size='340' side='right' caption='[[1jrm]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1jrm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JRM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JRM FirstGlance]. <br>
<table><tr><td colspan='2'>[[1jrm]] is a 1 chain structure with sequence from [http://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=1JRM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JRM FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jrm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jrm RCSB], [http://www.ebi.ac.uk/pdbsum/1jrm PDBsum], [http://www.topsan.org/Proteins/NESGC/1jrm TOPSAN]</span></td></tr>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jrm OCA], [http://pdbe.org/1jrm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jrm RCSB], [http://www.ebi.ac.uk/pdbsum/1jrm PDBsum], [http://www.topsan.org/Proteins/NESGC/1jrm TOPSAN]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
Line 23: Line 23:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 1jrm" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Methanothermobacter thermautotrophicus]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Pineda-Lucena, A]]
[[Category: Pineda-Lucena, A]]

Revision as of 19:53, 10 September 2015

NMR structure of MTH0637. Ontario Centre for Structural Proteomics target MTH0637_1_104; Northeast Structural Genomics Target TT135NMR structure of MTH0637. Ontario Centre for Structural Proteomics target MTH0637_1_104; Northeast Structural Genomics Target TT135

Structural highlights

1jrm is a 1 chain structure with sequence from "methanobacterium_thermoautotrophicus"_(sic)_zeikus_and_wolfe_1972 "methanobacterium thermoautotrophicus" (sic) zeikus and wolfe 1972. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, TOPSAN

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 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.

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

  1. 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. An NMR approach to structural proteomics. Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1825-30. PMID:11854485 doi:10.1073/pnas.042684599
Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA