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{{STRUCTURE_4h2v|  PDB=4h2v  |  SCENE=  }}
==Crystal structure of Bradyrhizobium japonicum glycine:[carrier protein] ligase complexed with glycylated carrier protein==
===Crystal structure of Bradyrhizobium japonicum glycine:[carrier protein] ligase complexed with glycylated carrier protein===
<StructureSection load='4h2v' size='340' side='right' caption='[[4h2v]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
{{ABSTRACT_PUBMED_23541895}}
== Structural highlights ==
<table><tr><td colspan='2'>[[4h2v]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bradyrhizobium_japonicum_usda_110 Bradyrhizobium japonicum usda 110]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H2V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H2V FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=H2V:S-[2-({N-[(2S)-2-HYDROXY-3,3-DIMETHYL-4-(PHOSPHONOOXY)BUTANOYL]-BETA-ALANYL}AMINO)ETHYL]+AMINOETHANETHIOATE'>H2V</scene>, <scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mf2|3mf2]], [[4h2s|4h2s]], [[4h2t|4h2t]], [[4h2u|4h2u]], [[4h2w|4h2w]], [[4h2x|4h2x]], [[4h2y|4h2y]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bll0957 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224911 Bradyrhizobium japonicum USDA 110]), bsr0959 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224911 Bradyrhizobium japonicum USDA 110])</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=4h2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h2v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h2v RCSB], [http://www.ebi.ac.uk/pdbsum/4h2v PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Amino acid:[carrier protein] ligases (aa:CP ligases) are recently discovered enzymes that are highly similar to class II aminoacyl-tRNA synthetases (aaRSs). However, while aaRSs aminoacylate tRNA and supply building blocks for ribosomal translation, aa:CP ligases transfer activated amino acids to the phosphopantetheine group of small carrier proteins. We have solved the crystal structure of an aa:CP ligase complexed with the carrier protein (CP). The CP prosthetic group enters the active site from a different direction than tRNA in class II aaRS complexes through an idiosyncratic tunnel. CP binds to aa:CP ligase in a fundamentally different manner compared to tRNA binding by structurally closely related aaRSs. Based on crystallographic analysis, an enzyme of altered CP specificity was designed, and the mechanism of amino acid transfer to the prosthetic group was proposed. The presented study reveals how a conserved class II aaRS catalytic core can adapt to another function through minor structural alterations.


==Function==
Adaptation of Aminoacyl-tRNA Synthetase Catalytic Core to Carrier Protein Aminoacylation.,Mocibob M, Ivic N, Luic M, Weygand-Durasevic I Structure. 2013 Mar 26. pii: S0969-2126(13)00058-0. doi:, 10.1016/j.str.2013.02.017. PMID:23541895<ref>PMID:23541895</ref>
[[http://www.uniprot.org/uniprot/AACL1_BRAJA AACL1_BRAJA]] Catalyzes the ATP-dependent activation of L-glycine and its transfer to the phosphopantetheine prosthetic group covalently attached to the vicinal carrier protein bsr0959 of yet unknown function. May participate in nonribosomal peptide synthesis or related processes. L-alanine is a poor substrate whereas L-serine or D-amino acids are not substrates for ATP-dependent activation. Does not display tRNA aminoacylation activity. [[http://www.uniprot.org/uniprot/AACP1_BRAJA AACP1_BRAJA]] Aminoacyl carrier protein. Can be charged with L-glycine via the formation of a thioester bond between the amino acid and the 4'-phosphopantetheinyl prosthetic group, catalyzed by the bll0957 ligase.  


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[4h2v]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bradyrhizobium_japonicum_usda_110 Bradyrhizobium japonicum usda 110]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H2V OCA].
</div>
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:023541895</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Bradyrhizobium japonicum usda 110]]
[[Category: Bradyrhizobium japonicum usda 110]]
[[Category: Ivic, N.]]
[[Category: Ivic, N]]
[[Category: Luic, M.]]
[[Category: Luic, M]]
[[Category: Mocibob, M.]]
[[Category: Mocibob, M]]
[[Category: Weygand-Durasevic, I.]]
[[Category: Weygand-Durasevic, I]]
[[Category: Aminoacyl-trna synthetase]]
[[Category: Aminoacyl-trna synthetase]]
[[Category: Atp binding]]
[[Category: Atp binding]]

Revision as of 14:08, 21 December 2014

Crystal structure of Bradyrhizobium japonicum glycine:[carrier protein] ligase complexed with glycylated carrier proteinCrystal structure of Bradyrhizobium japonicum glycine:[carrier protein] ligase complexed with glycylated carrier protein

Structural highlights

4h2v is a 4 chain structure with sequence from Bradyrhizobium japonicum usda 110. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , , , , ,
Gene:bll0957 (Bradyrhizobium japonicum USDA 110), bsr0959 (Bradyrhizobium japonicum USDA 110)
Resources:FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

Amino acid:[carrier protein] ligases (aa:CP ligases) are recently discovered enzymes that are highly similar to class II aminoacyl-tRNA synthetases (aaRSs). However, while aaRSs aminoacylate tRNA and supply building blocks for ribosomal translation, aa:CP ligases transfer activated amino acids to the phosphopantetheine group of small carrier proteins. We have solved the crystal structure of an aa:CP ligase complexed with the carrier protein (CP). The CP prosthetic group enters the active site from a different direction than tRNA in class II aaRS complexes through an idiosyncratic tunnel. CP binds to aa:CP ligase in a fundamentally different manner compared to tRNA binding by structurally closely related aaRSs. Based on crystallographic analysis, an enzyme of altered CP specificity was designed, and the mechanism of amino acid transfer to the prosthetic group was proposed. The presented study reveals how a conserved class II aaRS catalytic core can adapt to another function through minor structural alterations.

Adaptation of Aminoacyl-tRNA Synthetase Catalytic Core to Carrier Protein Aminoacylation.,Mocibob M, Ivic N, Luic M, Weygand-Durasevic I Structure. 2013 Mar 26. pii: S0969-2126(13)00058-0. doi:, 10.1016/j.str.2013.02.017. PMID:23541895[1]

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

References

  1. ↑ Mocibob M, Ivic N, Luic M, Weygand-Durasevic I. Adaptation of Aminoacyl-tRNA Synthetase Catalytic Core to Carrier Protein Aminoacylation. Structure. 2013 Mar 26. pii: S0969-2126(13)00058-0. doi:, 10.1016/j.str.2013.02.017. PMID:23541895 doi:10.1016/j.str.2013.02.017

4h2v, resolution 2.00Å

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