2x9q

From Proteopedia

(Difference between revisions)

Revision as of 10:48, 13 April 2022

Structure of the Mycobacterium tuberculosis protein, Rv2275, demonstrates that cyclodipeptide synthetases are related to type I tRNA-Synthetases.

Structural highlights

2x9q is a 2 chain structure with sequence from Myctu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CDTS_MYCTU] Involved in the biosynthesis of mycocyclosin. It uses activated amino acids in the form of aminoacyl-tRNAs (aa-tRNAs) as substrates to catalyze the ATP-independent formation of cyclodipeptides which are intermediates in diketopiperazine (DKP) biosynthetic pathways. Catalyzes the formation of cyclo(L-Tyr-L-Tyr) (cYY) from L-tyrosyl-tRNA(Tyr). Can incorporate various nonpolar residues, such as L-phenylalanine, L-leucine, L-tyrosine and L-methionine, and to a much lesser extent L-alanine, into cyclodipeptides. Cyclodipeptides synthesized by Rv2275 always contain L-tyrosine.^[1]

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 Mycobacterium tuberculosis enzyme Rv2275 catalyzes the formation of cyclo(L-Tyr-L-Tyr) using two molecules of Tyr-tRNA(Tyr) as substrates. The three-dimensional (3D) structure of Rv2275 was determined to 2.0-A resolution, revealing that Rv2275 is structurally related to the class Ic aminoacyl-tRNA synthetase family of enzymes. Mutagenesis and radioactive labeling suggests a covalent intermediate in which L-tyrosine is transferred from Tyr-tRNA(Tyr) to an active site serine (Ser88) by transesterification with Glu233 serving as a critical base, catalyzing dipeptide bond formation.

The structure and mechanism of the Mycobacterium tuberculosis cyclodityrosine synthetase.,Vetting MW, Hegde SS, Blanchard JS Nat Chem Biol. 2010 Sep 19. PMID:20852636^[2]

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

References

↑ Gondry M, Sauguet L, Belin P, Thai R, Amouroux R, Tellier C, Tuphile K, Jacquet M, Braud S, Courcon M, Masson C, Dubois S, Lautru S, Lecoq A, Hashimoto S, Genet R, Pernodet JL. Cyclodipeptide synthases are a family of tRNA-dependent peptide bond-forming enzymes. Nat Chem Biol. 2009 Jun;5(6):414-20. doi: 10.1038/nchembio.175. PMID:19430487 doi:http://dx.doi.org/10.1038/nchembio.175
↑ Vetting MW, Hegde SS, Blanchard JS. The structure and mechanism of the Mycobacterium tuberculosis cyclodityrosine synthetase. Nat Chem Biol. 2010 Sep 19. PMID:20852636 doi:10.1038/nchembio.440

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2x9q"

@@ Line 3: / Line 3: @@
 <StructureSection load='2x9q' size='340' side='right'caption='[[2x9q]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2x9q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X9Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2X9Q FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2x9q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X9Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X9Q FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=2x9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x9q OCA], [http://pdbe.org/2x9q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x9q RCSB], [http://www.ebi.ac.uk/pdbsum/2x9q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x9q ProSAT]</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=2x9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x9q OCA], [https://pdbe.org/2x9q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x9q RCSB], [https://www.ebi.ac.uk/pdbsum/2x9q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x9q ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CDTS_MYCTU CDTS_MYCTU]] Involved in the biosynthesis of mycocyclosin. It uses activated amino acids in the form of aminoacyl-tRNAs (aa-tRNAs) as substrates to catalyze the ATP-independent formation of cyclodipeptides which are intermediates in diketopiperazine (DKP) biosynthetic pathways. Catalyzes the formation of cyclo(L-Tyr-L-Tyr) (cYY) from L-tyrosyl-tRNA(Tyr). Can incorporate various nonpolar residues, such as L-phenylalanine, L-leucine, L-tyrosine and L-methionine, and to a much lesser extent L-alanine, into cyclodipeptides. Cyclodipeptides synthesized by Rv2275 always contain L-tyrosine.<ref>PMID:19430487</ref>
+[[https://www.uniprot.org/uniprot/CDTS_MYCTU CDTS_MYCTU]] Involved in the biosynthesis of mycocyclosin. It uses activated amino acids in the form of aminoacyl-tRNAs (aa-tRNAs) as substrates to catalyze the ATP-independent formation of cyclodipeptides which are intermediates in diketopiperazine (DKP) biosynthetic pathways. Catalyzes the formation of cyclo(L-Tyr-L-Tyr) (cYY) from L-tyrosyl-tRNA(Tyr). Can incorporate various nonpolar residues, such as L-phenylalanine, L-leucine, L-tyrosine and L-methionine, and to a much lesser extent L-alanine, into cyclodipeptides. Cyclodipeptides synthesized by Rv2275 always contain L-tyrosine.<ref>PMID:19430487</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2x9q

From Proteopedia

Revision as of 10:48, 13 April 2022

Structure of the Mycobacterium tuberculosis protein, Rv2275, demonstrates that cyclodipeptide synthetases are related to type I tRNA-Synthetases.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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