2V0N: Activated Response Regulator Pled In Complex With C-Digmp And Gtp-Alpha-S

Citation:
Abstract
Cyclic di-guanosine monophosphate (c-di-GMP) is a ubiquitous bacterial second messenger involved in the regulation of cell surface-associated traits and persistence. We have determined the crystal structure of PleD from Caulobacter crescentus, a response regulator with a diguanylate cyclase (DGC) domain, in its activated form. The BeF(3)(-) modification of its receiver domain causes rearrangement with respect to an adaptor domain, which, in turn, promotes dimer formation, allowing for the efficient encounter of two symmetric catalytic domains. The substrate analog GTPalphaS and two putative cations are bound to the active sites in a manner similar to adenylate cyclases, suggesting an analogous two-metal catalytic mechanism. An allosteric c-di-GMP-binding mode that crosslinks DGC and an adaptor domain had been identified before. Here, a second mode is observed that crosslinks the DGC domains within a PleD dimer. Both modes cause noncompetitive product inhibition by domain immobilization.
PDB ID: 2V0NDownload
MMDB ID: 59747
PDB Deposition Date: 2007/5/15
Updated in MMDB: 2009/10
Experimental Method:
x-ray diffraction
Resolution: 2.71  Å
Source Organism:
Similar Structures:
Biological Unit for 2V0N: dimeric; determined by author and by software (PISA)
Molecular Components in 2V0N
Label Count Molecule
Proteins (2 molecules)
2
Response Regulator Pled(Gene symbol: pleD)
Molecule annotation
Chemicals (16 molecules)
1
2
2
5
3
4
4
2
5
2
6
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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