1fo5: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (14 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
< | ==SOLUTION STRUCTURE OF REDUCED MJ0307== | ||
<StructureSection load='1fo5' size='340' side='right'caption='[[1fo5]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fo5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FO5 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=1fo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo5 OCA], [https://pdbe.org/1fo5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fo5 RCSB], [https://www.ebi.ac.uk/pdbsum/1fo5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fo5 ProSAT], [https://www.topsan.org/Proteins/BSGC/1fo5 TOPSAN]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/THIO_METJA THIO_METJA] Acts to maintain redox homeostasis; functions as a protein disulfide reductase. | |||
== 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/fo/1fo5_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=1fo5 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The solution structure of the protein disulfide oxidoreductase Mj0307 in the reduced form has been solved by nuclear magnetic resonance. The secondary and tertiary structure of this protein from the archaebacterium Methanococcus jannaschii is similar to the structures that have been solved for the glutaredoxin proteins from Escherichia coli, although Mj0307 also shows features that are characteristic of thioredoxin proteins. Some aspects of Mj0307's unique behavior can be explained by comparing structure-based sequence alignments with mesophilic bacterial and eukaryotic glutaredoxin and thioredoxin proteins. It is proposed that Mj0307, and similar archaebacterial proteins, may be most closely related to the mesophilic bacterial NrdH proteins. Together these proteins may form a unique subgroup within the family of protein disulfide oxidoreductases. | |||
Solution nuclear magnetic resonance structure of a protein disulfide oxidoreductase from Methanococcus jannaschii.,Cave JW, Cho HS, Batchelder AM, Yokota H, Kim R, Wemmer DE Protein Sci. 2001 Feb;10(2):384-96. PMID:11266624<ref>PMID:11266624</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1fo5" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Protein disulfide oxidoreductase 3D structures|Protein disulfide oxidoreductase 3D structures]] | |||
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
== | </StructureSection> | ||
[[Category: Large Structures]] | |||
== | |||
[[Category: Methanocaldococcus jannaschii]] | [[Category: Methanocaldococcus jannaschii]] | ||
[[Category: Batchelder AM]] | |||
[[Category: Batchelder | [[Category: Cave JW]] | ||
[[Category: Cave | [[Category: Cho HS]] | ||
[[Category: Cho | [[Category: Kim R]] | ||
[[Category: Kim | [[Category: Wemmer DE]] | ||
[[Category: Wemmer | [[Category: Yokota H]] | ||
[[Category: Yokota | |||
Latest revision as of 11:29, 22 May 2024
SOLUTION STRUCTURE OF REDUCED MJ0307SOLUTION STRUCTURE OF REDUCED MJ0307
Structural highlights
FunctionTHIO_METJA Acts to maintain redox homeostasis; functions as a protein disulfide reductase. 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 solution structure of the protein disulfide oxidoreductase Mj0307 in the reduced form has been solved by nuclear magnetic resonance. The secondary and tertiary structure of this protein from the archaebacterium Methanococcus jannaschii is similar to the structures that have been solved for the glutaredoxin proteins from Escherichia coli, although Mj0307 also shows features that are characteristic of thioredoxin proteins. Some aspects of Mj0307's unique behavior can be explained by comparing structure-based sequence alignments with mesophilic bacterial and eukaryotic glutaredoxin and thioredoxin proteins. It is proposed that Mj0307, and similar archaebacterial proteins, may be most closely related to the mesophilic bacterial NrdH proteins. Together these proteins may form a unique subgroup within the family of protein disulfide oxidoreductases. Solution nuclear magnetic resonance structure of a protein disulfide oxidoreductase from Methanococcus jannaschii.,Cave JW, Cho HS, Batchelder AM, Yokota H, Kim R, Wemmer DE Protein Sci. 2001 Feb;10(2):384-96. PMID:11266624[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||