4zvh: Difference between revisions
m Protected "4zvh" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of GGDEF domain of the E. coli DosC - form IV== | |||
<StructureSection load='4zvh' size='340' side='right' caption='[[4zvh]], [[Resolution|resolution]] 3.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4zvh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZVH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZVH FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dosC, Z2219, ECs2095 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Diguanylate_cyclase Diguanylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.65 2.7.7.65] </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=4zvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zvh OCA], [http://pdbe.org/4zvh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zvh RCSB], [http://www.ebi.ac.uk/pdbsum/4zvh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zvh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/DOSC_ECO57 DOSC_ECO57]] Globin-coupled heme-based oxygen sensor protein displaying diguanylate cyclase (DGC) activity in response to oxygen availability. Thus, catalyzes the synthesis of cyclic diguanylate (c-di-GMP) via the condensation of 2 GTP molecules. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cyclic di-GMP is a bacterial second messenger that is involved in switching between motile and sessile lifestyles. Given the medical importance of biofilm formation, there has been increasing interest in understanding the synthesis and degradation of cyclic di-GMPs and their regulation in various bacterial pathogens. Environmental cues are detected by sensing domains coupled to GGDEF and EAL or HD-GYP domains that have diguanylate cyclase and phosphodiesterase activities, respectively, producing and degrading cyclic di-GMP. The Escherichia coli protein DosC (also known as YddV) consists of an oxygen-sensing domain belonging to the class of globin sensors that is coupled to a C-terminal GGDEF domain via a previously uncharacterized middle domain. DosC is one of the most strongly expressed GGDEF proteins in E. coli, but to date structural information on this and related proteins is scarce. Here, the high-resolution structural characterization of the oxygen-sensing globin domain, the middle domain and the catalytic GGDEF domain in apo and substrate-bound forms is described. The structural changes between the iron(III) and iron(II) forms of the sensor globin domain suggest a mechanism for oxygen-dependent regulation. The structural information on the individual domains is combined into a model of the dimeric DosC holoprotein. These findings have direct implications for the oxygen-dependent regulation of the activity of the cyclase domain. | |||
Structural analysis of an oxygen-regulated diguanylate cyclase.,Tarnawski M, Barends TR, Schlichting I Acta Crystallogr D Biol Crystallogr. 2015 Nov;71(Pt 11):2158-77. doi:, 10.1107/S139900471501545X. Epub 2015 Oct 27. PMID:26527135<ref>PMID:26527135</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Barends, T | <div class="pdbe-citations 4zvh" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Diguanylate cyclase]] | |||
[[Category: Ecoli]] | |||
[[Category: Barends, T R.M]] | |||
[[Category: Schlichting, I]] | |||
[[Category: Tarnawski, M]] | [[Category: Tarnawski, M]] | ||
[[Category: | [[Category: Cyclic-di-gmp]] | ||
[[Category: Oxygen sensing]] | |||
[[Category: Signaling protein]] | |||
Revision as of 16:55, 16 November 2017
Crystal structure of GGDEF domain of the E. coli DosC - form IVCrystal structure of GGDEF domain of the E. coli DosC - form IV
Structural highlights
Function[DOSC_ECO57] Globin-coupled heme-based oxygen sensor protein displaying diguanylate cyclase (DGC) activity in response to oxygen availability. Thus, catalyzes the synthesis of cyclic diguanylate (c-di-GMP) via the condensation of 2 GTP molecules. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria (By similarity). Publication Abstract from PubMedCyclic di-GMP is a bacterial second messenger that is involved in switching between motile and sessile lifestyles. Given the medical importance of biofilm formation, there has been increasing interest in understanding the synthesis and degradation of cyclic di-GMPs and their regulation in various bacterial pathogens. Environmental cues are detected by sensing domains coupled to GGDEF and EAL or HD-GYP domains that have diguanylate cyclase and phosphodiesterase activities, respectively, producing and degrading cyclic di-GMP. The Escherichia coli protein DosC (also known as YddV) consists of an oxygen-sensing domain belonging to the class of globin sensors that is coupled to a C-terminal GGDEF domain via a previously uncharacterized middle domain. DosC is one of the most strongly expressed GGDEF proteins in E. coli, but to date structural information on this and related proteins is scarce. Here, the high-resolution structural characterization of the oxygen-sensing globin domain, the middle domain and the catalytic GGDEF domain in apo and substrate-bound forms is described. The structural changes between the iron(III) and iron(II) forms of the sensor globin domain suggest a mechanism for oxygen-dependent regulation. The structural information on the individual domains is combined into a model of the dimeric DosC holoprotein. These findings have direct implications for the oxygen-dependent regulation of the activity of the cyclase domain. Structural analysis of an oxygen-regulated diguanylate cyclase.,Tarnawski M, Barends TR, Schlichting I Acta Crystallogr D Biol Crystallogr. 2015 Nov;71(Pt 11):2158-77. doi:, 10.1107/S139900471501545X. Epub 2015 Oct 27. PMID:26527135[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||