4zxv
From Proteopedia
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==Streptomyces peucetius nitrososynthase DnmZ in ligand-free state== | ==Streptomyces peucetius nitrososynthase DnmZ in ligand-free state== | ||
<StructureSection load='4zxv' size='340' side='right' caption='[[4zxv]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='4zxv' size='340' side='right' caption='[[4zxv]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4zxv]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZXV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZXV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zxv]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1799 As 4.1799]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZXV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZXV FirstGlance]. <br> |
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zyj|4zyj]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zyj|4zyj]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dnmZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1950 AS 4.1799])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-evernosamine_nitrososynthase L-evernosamine nitrososynthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.187 1.14.13.187] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-evernosamine_nitrososynthase L-evernosamine nitrososynthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.187 1.14.13.187] </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=4zxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zxv OCA], [http://pdbe.org/4zxv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zxv RCSB], [http://www.ebi.ac.uk/pdbsum/4zxv PDBsum]</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=4zxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zxv OCA], [http://pdbe.org/4zxv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zxv RCSB], [http://www.ebi.ac.uk/pdbsum/4zxv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zxv ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Two-component signal transduction is the major signaling mechanism that enables bacteria to survive and thrive in complex environmental conditions. The photosynthetic bacterium R. palustris employs two tandem bacteriophytochromes, RpBphP2 and RpBphP3, to perceive red-light signals that regulate the synthesis of light-harvesting complexes under low-light conditions. Both RpBphP2 and RpBphP3 are photosensory histidine kinases coupled to the same response regulator RPA3017. Together, they constitute a two-component system that converts a red-light signal into a biological signal. In this work, the crystal structure of RPA3017 in the unphosphorylated form at 1.9 A resolution is presented. This structure reveals a tightly associated dimer arrangement that is conserved among phytochrome-related response regulators. The conserved active-site architecture provides structural insight into the phosphotransfer reaction between RpBphP2/RpBphP3 and RPA3017. Based on structural comparisons and homology modeling, how specific recognition between RpBphP2/RpBphP3 and RPA3017 is achieved at the molecular level is further explored. | ||
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| + | Structure of the response regulator RPA3017 involved in red-light signaling in Rhodopseudomonas palustris.,Yang X, Zeng X, Moffat K, Yang X Acta Crystallogr F Struct Biol Commun. 2015 Oct;71(Pt 10):1215-22. doi:, 10.1107/S2053230X15014661. Epub 2015 Sep 23. PMID:26457509<ref>PMID:26457509</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4zxv" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: As 4 1799]] | ||
[[Category: L-evernosamine nitrososynthase]] | [[Category: L-evernosamine nitrososynthase]] | ||
[[Category: Sartor, L M]] | [[Category: Sartor, L M]] | ||
Revision as of 06:17, 18 April 2018
Streptomyces peucetius nitrososynthase DnmZ in ligand-free state
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