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< | ==SOLUTION STRUCTURE OF A 8.3 KDA PROTEIN (GENE MTH1184) FROM METHANOBACTERIUM THERMOAUTOTROPHICUM== | ||
<StructureSection load='1gh9' size='340' side='right'caption='[[1gh9]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1gh9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1dw7 1dw7]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GH9 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=1gh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gh9 OCA], [https://pdbe.org/1gh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gh9 RCSB], [https://www.ebi.ac.uk/pdbsum/1gh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gh9 ProSAT], [https://www.topsan.org/Proteins/NESGC/1gh9 TOPSAN]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PA84_METTH PA84_METTH] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A set of 424 nonmembrane proteins from Methanobacterium thermoautotrophicum were cloned, expressed and purified for structural studies. Of these, approximately 20% were found to be suitable candidates for X-ray crystallographic or NMR spectroscopic analysis without further optimization of conditions, providing an estimate of the number of the most accessible structural targets in the proteome. A retrospective analysis of the experimental behavior of these proteins suggested some simple relations between sequence and solubility, implying that data bases of protein properties will be useful in optimizing high throughput strategies. Of the first 10 structures determined, several provided clues to biochemical functions that were not detectable from sequence analysis, and in many cases these putative functions could be readily confirmed by biochemical methods. This demonstrates that structural proteomics is feasible and can play a central role in functional genomics. | |||
Structural proteomics of an archaeon.,Christendat D, Yee A, Dharamsi A, Kluger Y, Savchenko A, Cort JR, Booth V, Mackereth CD, Saridakis V, Ekiel I, Kozlov G, Maxwell KL, Wu N, McIntosh LP, Gehring K, Kennedy MA, Davidson AR, Pai EF, Gerstein M, Edwards AM, Arrowsmith CH Nat Struct Biol. 2000 Oct;7(10):903-9. PMID:11017201<ref>PMID:11017201</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1gh9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
--> | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: Methanothermobacter thermautotrophicus]] | [[Category: Methanothermobacter thermautotrophicus]] | ||
[[Category: Ekiel I]] | |||
[[Category: Ekiel | [[Category: Gehring K]] | ||
[[Category: Gehring | [[Category: Kozlov G]] | ||
[[Category: Kozlov | |||
Latest revision as of 21:37, 29 November 2023
SOLUTION STRUCTURE OF A 8.3 KDA PROTEIN (GENE MTH1184) FROM METHANOBACTERIUM THERMOAUTOTROPHICUMSOLUTION STRUCTURE OF A 8.3 KDA PROTEIN (GENE MTH1184) FROM METHANOBACTERIUM THERMOAUTOTROPHICUM
Structural highlights
FunctionPublication Abstract from PubMedA set of 424 nonmembrane proteins from Methanobacterium thermoautotrophicum were cloned, expressed and purified for structural studies. Of these, approximately 20% were found to be suitable candidates for X-ray crystallographic or NMR spectroscopic analysis without further optimization of conditions, providing an estimate of the number of the most accessible structural targets in the proteome. A retrospective analysis of the experimental behavior of these proteins suggested some simple relations between sequence and solubility, implying that data bases of protein properties will be useful in optimizing high throughput strategies. Of the first 10 structures determined, several provided clues to biochemical functions that were not detectable from sequence analysis, and in many cases these putative functions could be readily confirmed by biochemical methods. This demonstrates that structural proteomics is feasible and can play a central role in functional genomics. Structural proteomics of an archaeon.,Christendat D, Yee A, Dharamsi A, Kluger Y, Savchenko A, Cort JR, Booth V, Mackereth CD, Saridakis V, Ekiel I, Kozlov G, Maxwell KL, Wu N, McIntosh LP, Gehring K, Kennedy MA, Davidson AR, Pai EF, Gerstein M, Edwards AM, Arrowsmith CH Nat Struct Biol. 2000 Oct;7(10):903-9. PMID:11017201[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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