6ulz: Difference between revisions

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<StructureSection load='6ulz' size='340' side='right'caption='[[6ulz]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
<StructureSection load='6ulz' size='340' side='right'caption='[[6ulz]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6ulz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10027 Atcc 10027]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ULZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ULZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[6ulz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10027 Atcc 10027]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ULZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ULZ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=KIV:3-METHYL-2-OXOBUTANOIC+ACID'>KIV</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=KIV:3-METHYL-2-OXOBUTANOIC+ACID'>KIV</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lgrA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=54914 ATCC 10027])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lgrA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=54914 ATCC 10027])</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=6ulz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ulz OCA], [http://pdbe.org/6ulz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ulz RCSB], [http://www.ebi.ac.uk/pdbsum/6ulz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ulz 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=6ulz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ulz OCA], [http://pdbe.org/6ulz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ulz RCSB], [http://www.ebi.ac.uk/pdbsum/6ulz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ulz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==

Revision as of 09:37, 6 May 2020

Adenylation domain of the initiation module of LgrA mutant P483MAdenylation domain of the initiation module of LgrA mutant P483M

Structural highlights

6ulz is a 1 chain structure with sequence from Atcc 10027. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:lgrA (ATCC 10027)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LGRA_BREPA] Activates valine (or leucine, but much less frequently), and then glycine and catalyzes the formation of the peptide bond in the first step of peptide synthesis. This enzyme may also play a role in N-formylation of the first amino acid residue in the synthesized dipeptide.

Publication Abstract from PubMed

Nonribosomal depsipeptides are natural products composed of amino and hydroxy acid residues. The hydroxy acid residues often derive from alpha-keto acids, reduced by ketoreductase domains in the depsipeptide synthetases. Biochemistry and structures reveal the mechanism of discrimination for alpha-keto acids and a remarkable architecture: flanking intact adenylation and ketoreductase domains are sequences separated by >1,100 residues that form a split 'pseudoAsub' domain, structurally important for the depsipeptide module's synthetic cycle.

Structural basis of keto acid utilization in nonribosomal depsipeptide synthesis.,Alonzo DA, Chiche-Lapierre C, Tarry MJ, Wang J, Schmeing TM Nat Chem Biol. 2020 Feb 17. pii: 10.1038/s41589-020-0481-5. doi:, 10.1038/s41589-020-0481-5. PMID:32066969[1]

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

References

  1. Alonzo DA, Chiche-Lapierre C, Tarry MJ, Wang J, Schmeing TM. Structural basis of keto acid utilization in nonribosomal depsipeptide synthesis. Nat Chem Biol. 2020 Feb 17. pii: 10.1038/s41589-020-0481-5. doi:, 10.1038/s41589-020-0481-5. PMID:32066969 doi:http://dx.doi.org/10.1038/s41589-020-0481-5

6ulz, resolution 3.10Å

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OCA