User:Nane Milene Sposito Almeida Pereira/Sandbox 1

From Proteopedia

< User:Nane Milene Sposito Almeida Pereira(Difference between revisions)
Jump to: navigation, search
Current revision (03:10, 22 June 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 11: Line 11:
The crystal structure of full-lenght SiaD in complex with SiaC was determined by integrating the diffraction data and scaling them using the program HKL3000 to space group C2221 at 2.65 Å resolution, and the structure was subsequently determined through molecular replacement using the published conserved DGC domain of the [[WspR]] structure (PDB code: 3BRE) and the SiaC structure (PDB code: 6KKP).
The crystal structure of full-lenght SiaD in complex with SiaC was determined by integrating the diffraction data and scaling them using the program HKL3000 to space group C2221 at 2.65 Å resolution, and the structure was subsequently determined through molecular replacement using the published conserved DGC domain of the [[WspR]] structure (PDB code: 3BRE) and the SiaC structure (PDB code: 6KKP).
 +
 +
The accuracy of SiaC–SiaD complex conformation obtained from the structure was further confirmed using the synchrotron-based solution small angle X-ray scattering (SAXS) and the result suggested consistency between the experimental scattering intensity and the crystal structure model.
'''The DGC domain of SiaD'''
'''The DGC domain of SiaD'''
-
The C-terminal GGDEF domain of SiaD is highly conserved. Two DGC domains in the complex are oriented anti-parallel, with their active sites facing each other. Each DGC domain consists of a core canonical fold of five antiparallel β-strands (β1–β5) around which five α-helices (α0–α4) and two short antiparallel β-strands are wrapped (β3ʹ and β3"), forming a highly conserved GTP substrate-binding site (GGDEF domain, A-site) and a c-di-GMP product binding/inhibitory site (I-site). [[Image:Overview_of_the_DGC_domain_dimer.jpg|500px|left|thumb| Overview of the DGC domain dimer. A-site and I-site were labeled, respectively [3]]]
+
The C-terminal GGDEF domain of SiaD is highly conserved. Two DGC domains in the complex are oriented anti-parallel, with their active sites facing each other. Each DGC domain consists of a core canonical fold of five antiparallel β-strands (β1–β5) around which five α-helices (α0–α4) and two short antiparallel β-strands are wrapped (β3ʹ and β3"), forming a highly conserved GTP substrate-binding site (GGDEF domain, A-site) and a c-di-GMP product binding/inhibitory site (I-site). [[Image:Overview_of_the_DGC_domain_dimer.jpg|500px|left|thumb| Overview of the DGC domain dimer. A-site and I-site were labeled, respectively [1]]]
-
 
+
-
Furthermore, residues involved in GTP and Mg 2+ binding have been shown to be essential for the DGC activity of SiaD. [[Image:GpCpp_SiaD_(A-site).jpg|220px|center|thumb| GpCpp binds to the C-terminal DGC domain of SiaD (A-site) [3]]]
+
-
 
+
-
 
+
-
== Relevance ==
+
-
In Pseudomonas aeruginosa, the SiaA/B/C/D signaling network regulates biofilm and aggregate formation in response to environmental stimuli.
+
 +
Furthermore, residues involved in GTP and Mg 2+ binding have been shown to be essential for the DGC activity of SiaD. [[Image:GpCpp_SiaD_(A-site).jpg|220px|center|thumb| GpCpp binds to the C-terminal DGC domain of SiaD (A-site) [1]]]

Current revision

SiaC-SiaD Complex

Crystal structure of diguanylate cyclase SiaD in complex with its activator SiaC from Pseudomonas aeruginosa (PDB entry 7E6G)

Drag the structure with the mouse to rotate

References

  1. ↑ Chen G, Zhou J, Zuo Y, Huo W, Peng J, Li M, Zhang Y, Wang T, Zhang L, Zhang L, Liang H. Structural basis for diguanylate cyclase activation by its binding partner in Pseudomonas aeruginosa. Elife. 2021 Sep 9;10:e67289. PMID:34498587 doi:10.7554/eLife.67289

Proteopedia Page Contributors and Editors (what is this?)

Nane Milene Sposito Almeida Pereira

Retrieved from "http://52.214.119.220/wiki/index.php/User:Nane_Milene_Sposito_Almeida_Pereira/Sandbox_1"
Personal tools