1gh9: Difference between revisions

Revision as of 05:16, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1gh9.png

Template:STRUCTURE 1gh9

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

Template:ABSTRACT PUBMED 11017201

About this StructureAbout this Structure

1GH9 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. This structure supersedes the now removed PDB entry 1dw7. Full experimental information is available from OCA.

ReferenceReference

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

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

OCA

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-'''SOLUTION STRUCTURE OF A 8.3 KDA PROTEIN (GENE MTH1184) FROM METHANOBACTERIUM THERMOAUTOTROPHICUM'''
+===SOLUTION STRUCTURE OF A 8.3 KDA PROTEIN (GENE MTH1184) FROM METHANOBACTERIUM THERMOAUTOTROPHICUM===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11017201}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11017201 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11017201}}
 ==About this Structure==
-GH9 is a [[Single protein]] structure of sequence from [http://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 crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GH9 OCA].
+GH9 is a [[Single protein]] structure of sequence from [http://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].
 ==Reference==
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 [[Category: Psi]]
 [[Category: Structural genomic]]
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