2odr: Difference between revisions

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==Methanococcus Maripaludis Phosphoseryl-tRNA synthetase==
==Methanococcus Maripaludis Phosphoseryl-tRNA synthetase==
<StructureSection load='2odr' size='340' side='right' caption='[[2odr]], [[Resolution|resolution]] 3.23&Aring;' scene=''>
<StructureSection load='2odr' size='340' side='right'caption='[[2odr]], [[Resolution|resolution]] 3.23&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2odr]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Metmp Metmp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ODR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ODR FirstGlance]. <br>
<table><tr><td colspan='2'>[[2odr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanococcus_maripaludis_S2 Methanococcus maripaludis S2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ODR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ODR FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.228&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MMP0688 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=267377 METMP])</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=2odr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2odr OCA], [https://pdbe.org/2odr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2odr RCSB], [https://www.ebi.ac.uk/pdbsum/2odr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2odr ProSAT]</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=2odr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2odr OCA], [http://pdbe.org/2odr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2odr RCSB], [http://www.ebi.ac.uk/pdbsum/2odr PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SEPS_METMP SEPS_METMP]] Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys).[HAMAP-Rule:MF_01674]  
[https://www.uniprot.org/uniprot/SEPS_METMP SEPS_METMP] Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys).[HAMAP-Rule:MF_01674]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/od/2odr_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/od/2odr_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=2odr ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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==See Also==
==See Also==
*[[Aminoacyl tRNA Synthetase|Aminoacyl tRNA Synthetase]]
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Metmp]]
[[Category: Large Structures]]
[[Category: Kamtekar, S]]
[[Category: Methanococcus maripaludis S2]]
[[Category: Steitz, T A]]
[[Category: Kamtekar S]]
[[Category: Ligase]]
[[Category: Steitz TA]]
[[Category: Phosphoserine trna synthetase class ii]]

Latest revision as of 03:17, 28 December 2023

Methanococcus Maripaludis Phosphoseryl-tRNA synthetaseMethanococcus Maripaludis Phosphoseryl-tRNA synthetase

Structural highlights

2odr is a 4 chain structure with sequence from Methanococcus maripaludis S2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.228Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SEPS_METMP Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys).[HAMAP-Rule:MF_01674]

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

A number of archaeal organisms generate Cys-tRNA(Cys) in a two-step pathway, first charging phosphoserine (Sep) onto tRNA(Cys) and subsequently converting it to Cys-tRNA(Cys). We have determined, at 3.2-A resolution, the structure of the Methanococcus maripaludis phosphoseryl-tRNA synthetase (SepRS), which catalyzes the first step of this pathway. The structure shows that SepRS is a class II, alpha(4) synthetase whose quaternary structure arrangement of subunits closely resembles that of the heterotetrameric (alphabeta)(2) phenylalanyl-tRNA synthetase (PheRS). Homology modeling of a tRNA complex indicates that, in contrast to PheRS, a single monomer in the SepRS tetramer may recognize both the acceptor terminus and anticodon of a tRNA substrate. Using a complex with tungstate as a marker for the position of the phosphate moiety of Sep, we suggest that SepRS and PheRS bind their respective amino acid substrates in dissimilar orientations by using different residues.

Toward understanding phosphoseryl-tRNACys formation: the crystal structure of Methanococcus maripaludis phosphoseryl-tRNA synthetase.,Kamtekar S, Hohn MJ, Park HS, Schnitzbauer M, Sauerwald A, Soll D, Steitz TA Proc Natl Acad Sci U S A. 2007 Feb 20;104(8):2620-5. Epub 2007 Feb 14. PMID:17301225[1]

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

See Also

References

  1. Kamtekar S, Hohn MJ, Park HS, Schnitzbauer M, Sauerwald A, Soll D, Steitz TA. Toward understanding phosphoseryl-tRNACys formation: the crystal structure of Methanococcus maripaludis phosphoseryl-tRNA synthetase. Proc Natl Acad Sci U S A. 2007 Feb 20;104(8):2620-5. Epub 2007 Feb 14. PMID:17301225

2odr, resolution 3.23Å

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OCA