This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4hu4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:44, 1 March 2024) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 4hu4 is ON HOLD
+
==Crystal structure of EAL domain of the E. coli DosP - dimeric form==
-
 
+
<StructureSection load='4hu4' size='340' side='right'caption='[[4hu4]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-
Authors: Tarnawski, M., Barends, T.R.M., Hartmann, E., Schlichting, I.
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[4hu4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HU4 FirstGlance]. <br>
-
Description:
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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=4hu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hu4 OCA], [https://pdbe.org/4hu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hu4 RCSB], [https://www.ebi.ac.uk/pdbsum/4hu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hu4 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/DOSP_ECOLI DOSP_ECOLI] Heme-based oxygen sensor protein displaying phosphodiesterase (PDE) activity toward c-di-GMP in response to oxygen availability. Involved in the modulation of intracellular c-di-GMP levels, in association with DosC which catalyzes the biosynthesis of c-di-GMP (diguanylate cyclase activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Has very poor PDE activity on cAMP (PubMed:15995192) but is not active with cGMP, bis(p-nitrophenyl) phosphate or p-nitrophenyl phosphate (PubMed:11970957). Via its PDE activity on c-di-GMP, DosP regulates biofilm formation through the repression of transcription of the csgBAC operon, which encodes curli structural subunits.<ref>PMID:20553324</ref>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Escherichia coli K-12]]
 +
[[Category: Large Structures]]
 +
[[Category: Barends TRM]]
 +
[[Category: Hartmann E]]
 +
[[Category: Schlichting I]]
 +
[[Category: Tarnawski M]]

Current revision

Crystal structure of EAL domain of the E. coli DosP - dimeric form

PDB ID 4hu4

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools