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2x1m

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Current revision

Crystal structure of Mycobacterium smegmatis methionyl-tRNA synthetase in complex with methionine

Structural highlights

2x1m is a 1 chain structure with sequence from Mycolicibacterium smegmatis MC2 155. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.8Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0R3E2_MYCS2 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).[SAAS:SAAS023457_004_015657][HAMAP-Rule:MF_01228]

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

Two structures of monomeric methionyl-tRNA synthetase, from Mycobacterium smegmatis, in complex with the ligands methionine/adenosine and methionine, were analyzed by X-ray crystallography at 2.3 A and at 2.8 A, respectively. The structures demonstrated the flexibility of the multidomain enzyme. A new conformation of the structure was identified in which the connective peptide domain bound more closely to the catalytic domain than described previously. The KMSKS(301-305) loop in our structures was in an open and inactive conformation that differed from previous structures by a rotation of the loop of about 90 degrees around hinges located at Asn297 and Val310. The binding of adenosine to the methionyl-tRNA synthetase methionine complex caused a shift in the KMSKS domain that brought it closer to the catalytic domain. The potential use of the adenosine-binding site for inhibitor binding was evaluated and a potential binding site for a specific allosteric inhibitor was identified.

Flexibility and communication within the structure of the Mycobacterium smegmatis methionyl-tRNA synthetase.,Ingvarsson H, Unge T FEBS J. 2010 Aug 26. PMID:20796028^[1]

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

References

↑ Ingvarsson H, Unge T. Flexibility and communication within the structure of the Mycobacterium smegmatis methionyl-tRNA synthetase. FEBS J. 2010 Aug 26. PMID:20796028 doi:10.1111/j.1742-4658.2010.07784.x

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/2x1m"

Categories: Large Structures | Mycolicibacterium smegmatis MC2 155 | Ingvarsson H | Jones TA | Unge T

@@ Line 3: / Line 3: @@
 <StructureSection load='2x1m' size='340' side='right'caption='[[2x1m]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2x1m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X1M OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2X1M FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2x1m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X1M FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2HP:DIHYDROGENPHOSPHATE+ION'>2HP</scene>, <scene name='pdbligand=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</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]] 2.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2x1l|2x1l]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2HP:DIHYDROGENPHOSPHATE+ION'>2HP</scene>, <scene name='pdbligand=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=2x1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x1m OCA], [https://pdbe.org/2x1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x1m RCSB], [https://www.ebi.ac.uk/pdbsum/2x1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x1m ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2x1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x1m OCA], [http://pdbe.org/2x1m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x1m RCSB], [http://www.ebi.ac.uk/pdbsum/2x1m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x1m ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/A0R3E2_MYCS2 A0R3E2_MYCS2]] 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).[SAAS:SAAS023457_004_015657][HAMAP-Rule:MF_01228]
+[https://www.uniprot.org/uniprot/A0R3E2_MYCS2 A0R3E2_MYCS2] 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).[SAAS:SAAS023457_004_015657][HAMAP-Rule:MF_01228]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 38: / Line 37: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Methionine--tRNA ligase]]
+[[Category: Mycolicibacterium smegmatis MC2 155]]
-[[Category: Mycs2]]
+[[Category: Ingvarsson H]]
-[[Category: Ingvarsson, H]]
+[[Category: Jones TA]]
-[[Category: Jones, T A]]
+[[Category: Unge T]]
-[[Category: Unge, T]]
-[[Category: Aminoacyl-trna synthetase]]
-[[Category: Ligase]]
-[[Category: Nucleotide-binding]]
-[[Category: Protein biosynthesis]]

2x1m

From Proteopedia

Current revision

Crystal structure of Mycobacterium smegmatis methionyl-tRNA synthetase in complex with methionine

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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