1mkh

From Proteopedia

(Difference between revisions)

Revision as of 12:19, 10 September 2015

C-terminal domain of methionyl-tRNA synthetase from Pyrococcus abyssi

Structural highlights

1mkh is a 1 chain structure with sequence from "pyrococcus_abyssi"_erauso_et_al._1993 "pyrococcus abyssi" erauso et al. 1993. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	metG ("Pyrococcus abyssi" Erauso et al. 1993)
Activity:	Methionine--tRNA ligase, with EC number 6.1.1.10
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[SYM_PYRAB] Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation (By similarity).

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 minimal polypeptide supporting full methionyl-tRNA synthetase (MetRS) activity is composed of four domains: a catalytic Rossmann fold, a connective peptide, a KMSKS domain, and a C-terminal alpha helix bundle domain. The minimal MetRS behaves as a monomer. In several species, MetRS is a homodimer because of a C-terminal domain appended to the core polypeptide. Upon truncation of this C-terminal domain, subunits dissociate irreversibly. Here, the C-terminal domain of dimeric MetRS from Pyrococcus abyssi was isolated and studied. It displays nonspecific tRNA-binding properties and has a crystalline structure closely resembling that of Trbp111, a dimeric tRNA-binding protein found in many bacteria and archaea. The obtained 3D model was used to direct mutations against dimerization of Escherichia coli MetRS. Comparison of the resulting mutants to native and C-truncated MetRS shows that the presence of the appended C-domain improves tRNA(Met) binding affinity. However, dimer formation is required to evidence the gain in affinity.

Structure and function of the C-terminal domain of methionyl-tRNA synthetase.,Crepin T, Schmitt E, Blanquet S, Mechulam Y Biochemistry. 2002 Oct 29;41(43):13003-11. PMID:12390027^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Crepin T, Schmitt E, Blanquet S, Mechulam Y. Structure and function of the C-terminal domain of methionyl-tRNA synthetase. Biochemistry. 2002 Oct 29;41(43):13003-11. PMID:12390027

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mkh"

@@ Line 2: / Line 2: @@
 <StructureSection load='1mkh' size='340' side='right' caption='[[1mkh]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mkh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MKH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mkh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"pyrococcus_abyssi"_erauso_et_al._1993 "pyrococcus abyssi" erauso et al. 1993]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MKH FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">metG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29292 Pyrococcus abyssi])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">metG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29292 "Pyrococcus abyssi" Erauso et al. 1993])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine--tRNA_ligase Methionine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.10 6.1.1.10] </span></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=1mkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mkh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mkh RCSB], [http://www.ebi.ac.uk/pdbsum/1mkh PDBsum]</span></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=1mkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mkh OCA], [http://pdbe.org/1mkh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mkh RCSB], [http://www.ebi.ac.uk/pdbsum/1mkh PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1mkh" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 34: / Line 35: @@
 __TOC__
 </StructureSection>
+[[Category: Pyrococcus abyssi erauso et al. 1993]]
 [[Category: Methionine--tRNA ligase]]
-[[Category: Pyrococcus abyssi]]
 [[Category: Blanquet, S]]
 [[Category: Crepin, T]]

1mkh

From Proteopedia

Revision as of 12:19, 10 September 2015

C-terminal domain of methionyl-tRNA synthetase from Pyrococcus abyssi

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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