6ulx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='6ulx' size='340' side='right'caption='[[6ulx]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
<StructureSection load='6ulx' size='340' side='right'caption='[[6ulx]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6ulx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ULX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ULX FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6ulx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_stratosphericus_lama_585 Bacillus stratosphericus lama 585]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ULX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ULX FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=QA7:5-O-{(S)-hydroxy[(4-methyl-2-oxopentanoyl)oxy]phosphoryl}adenosine'>QA7</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=QA7:5-O-{(S)-hydroxy[(4-methyl-2-oxopentanoyl)oxy]phosphoryl}adenosine'>QA7</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C883_1060 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1236481 Bacillus stratosphericus LAMA 585])</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=6ulx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ulx OCA], [http://pdbe.org/6ulx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ulx RCSB], [http://www.ebi.ac.uk/pdbsum/6ulx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ulx ProSAT]</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=6ulx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ulx OCA], [http://pdbe.org/6ulx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ulx RCSB], [http://www.ebi.ac.uk/pdbsum/6ulx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ulx ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
-
phenix.refine is a program within the PHENIX package that supports crystallographic structure refinement against experimental data with a wide range of upper resolution limits using a large repertoire of model parameterizations. It has several automation features and is also highly flexible. Several hundred parameters enable extensive customizations for complex use cases. Multiple user-defined refinement strategies can be applied to specific parts of the model in a single refinement run. An intuitive graphical user interface is available to guide novice users and to assist advanced users in managing refinement projects. X-ray or neutron diffraction data can be used separately or jointly in refinement. phenix.refine is tightly integrated into the PHENIX suite, where it serves as a critical component in automated model building, final structure refinement, structure validation and deposition to the wwPDB. This paper presents an overview of the major phenix.refine features, with extensive literature references for readers interested in more detailed discussions of the methods.
+
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 &gt;1,100 residues that form a split 'pseudoAsub' domain, structurally important for the depsipeptide module's synthetic cycle.
-
Towards automated crystallographic structure refinement with phenix.refine.,Afonine PV, Grosse-Kunstleve RW, Echols N, Headd JJ, Moriarty NW, Mustyakimov M, Terwilliger TC, Urzhumtsev A, Zwart PH, Adams PD Acta Crystallogr D Biol Crystallogr. 2012 Apr;68(Pt 4):352-67. doi:, 10.1107/S0907444912001308. Epub 2012 Mar 16. PMID:22505256<ref>PMID:22505256</ref>
+
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<ref>PMID:32066969</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Line 20: Line 21:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Bacillus stratosphericus lama 585]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Alonzo, D A]]
[[Category: Alonzo, D A]]

Revision as of 07:21, 4 March 2020

Adenylation domain of a keto acid-selecting NRPS module bound to keto acyl adenylate space group P43212

PDB ID 6ulx

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6ulx"
Personal tools