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| | <StructureSection load='5isw' size='340' side='right'caption='[[5isw]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='5isw' size='340' side='right'caption='[[5isw]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5isw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_8246 Atcc 8246]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ISW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ISW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5isw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ISW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ISW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.75Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5isx|5isx]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">grsA, grs1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1393 ATCC 8246])</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=5isw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5isw OCA], [https://pdbe.org/5isw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5isw RCSB], [https://www.ebi.ac.uk/pdbsum/5isw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5isw ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phenylalanine_racemase_(ATP-hydrolyzing) Phenylalanine racemase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.11 5.1.1.11] </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=5isw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5isw OCA], [http://pdbe.org/5isw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5isw RCSB], [http://www.ebi.ac.uk/pdbsum/5isw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5isw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GRSA_BREBE GRSA_BREBE]] In the first step of peptide synthesis this enzyme activates phenylalanine and racemizes it to the D-isomer. | + | [https://www.uniprot.org/uniprot/GRSA_BREBE GRSA_BREBE] In the first step of peptide synthesis this enzyme activates phenylalanine and racemizes it to the D-isomer. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Nonribosomal peptide synthetases are large, complex multidomain enzymes responsible for the biosynthesis of a wide range of peptidic natural products. Inherent to synthetase chemistry is the thioester templated mechanism that relies on protein/protein interactions and interdomain dynamics. Several questions related to structure and mechanism remain to be addressed, including the incorporation of accessory domains and intermodule interactions. The inclusion of nonproteinogenic d-amino acids into peptide frameworks is a common and important modification for bioactive nonribosomal peptides. Epimerization domains, embedded in nonribosomal peptide synthetases assembly lines, catalyze the l- to d-amino acid conversion. Here we report the structure of the epimerization domain/peptidyl carrier protein didomain construct from the first module of the cyclic peptide antibiotic gramicidin synthetase. Both holo (phosphopantethiene post-translationally modified) and apo structures were determined, each representing catalytically relevant conformations of the two domains. The structures provide insight into domain-domain recognition, substrate delivery during the assembly line process, in addition to the structural organization of homologous condensation domains, canonical players in all synthetase modules.
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| - | Interdomain and Intermodule Organization in Epimerization Domain Containing Nonribosomal Peptide Synthetases.,Chen WH, Li K, Guntaka NS, Bruner SD ACS Chem Biol. 2016 Jun 24. PMID:27294598<ref>PMID:27294598</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 5isw" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 8246]] | + | [[Category: Brevibacillus brevis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bruner, S D]] | + | [[Category: Bruner SD]] |
| - | [[Category: Chen, W H]] | + | [[Category: Chen W-H]] |
| - | [[Category: Li, K]] | + | [[Category: Li K]] |
| - | [[Category: Epimerization domain]]
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| - | [[Category: Gramicidin s synthetase]]
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| - | [[Category: Isomerase]]
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| - | [[Category: Nrp]]
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