3MH7

Release Date:2010-06-30

Classification:Hydrolase

Experiment:X-RAY DIFFRACTION with resolution of 2.96 Å

Compound:2 Polymers

Molecule:Protease do

Polymer:1

Type:polypeptide(L)

Length:456

Chains:A

EC#:3.4.21.-

Mutation:S210A

Molecule:5-mer peptide

Polymer:2

Type:polypeptide(L)

Length:5

Chains:B, C

Other Details:
this peptide apparently picked up during protein purification.

3MH6

Release Date:2010-06-30
Classification:Hydrolase
Experiment:X-RAY DIFFRACTION with resolution of 3.60 Å
Compound:1 Polymer
Molecule:Protease do
Polymer:1
Type:polypeptide(L)
Length:456
Chains:A
EC#:3.4.21.- 1 Ligand

3GC0
Release Date:2009-03-31
Classification:Hydrolase/hydrolase Activator
Experiment:X-RAY DIFFRACTION with resolution of 2.80 Å
Compound:2 Polymers
Molecule:Protease degS
Polymer:1
Type:polypeptide(L)
Length:340

Chains:A
EC#:3.4.21.-
Mutation:H198P,D320A
Molecule:
DNRDGNVYQF peptide
Polymer:2
Type:
polypeptide(L)
Length:
10
Chains:
B
Citation:
OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism. (2009) Structure 17: 1411-1421

3GDS

Release Date:2009-03-31

Classification:Hydrolase/hydrolase Activator

Experiment:X-RAY DIFFRACTION with resolution of 2.85 Å
Compound:2 Polymers
Molecule:Protease degS
Polymer:1

Type:polypeptide(L)
Length:340
Chains:A
EC#:3.4.21.-
Fragment:full-length without membrane anchor
Mutation:H198P,D320A
Molecule:DNRDGNVYYF peptide
Polymer:2
Type:polypeptide(L)
Length:10
Chains:B
Citation:
OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism. (2009) Structure 17: 1411-1421
In the E. coli periplasm, C-terminal peptides of misfolded outer-membrane porins (OMPs) bind to the PDZ domains of the trimeric DegS protease, triggering cleavage of a transmembrane regulator and transcriptional activation of stress genes. We show that an active-site DegS mutation partially bypasses the requirement for peptide activation and acts synergistically with mutations that disrupt contacts between the protease and PDZ domains. Biochemical results support an allosteric model, in which these mutations, active-site modification, and peptide/substrate binding act in concert to stabilize proteolytically active DegS. Cocrystal structures of DegS in complex with different OMP peptides reveal activation of the protease domain with varied conformations of the PDZ domain and without specific contacts from the bound OMP peptide. Taken together, these results indicate that the binding of OMP peptides activates proteolysis principally by relieving inhibitory contacts between the PDZ domain and the protease domain of DegS. Citation Authors: Sohn, J., Grant, R.A., Sauer, R.T.

3B8J

Release Date:2008-09-16
Classification:Hydrolase

Experiment:X-RAY DIFFRACTION with resolution of 2.51 Å
Compound:1 Polymer

My journey of life

Assalamualaikum…

Shaking. This is my first time writing for the blog.hahaha.

My name is Muhammad Farhan bin Mahmud. I’m from kajang.26 august is my first registration in this world. I am friendly and joyful person. Now I’m at IIUM kuantan for my degree.

Math. Some people interest but not others. Different people different attitude. But, that is my course in IIUM kuantan. After some class I attend, I realized that math is not just playing with number, but also more to creative, understand and apply the concept. Honestly it is different from what I learn at the primary and secondary school, but it is totally different .Now, we have to read math, understand, try to proof it and apply in daily life.h0h0.quite interesting rite.? I will story about my Number Theory class. Full of headache and others killer virus. Class with DR Pah. But maybe next time. I’m quite tired now. I hope Allah will give strength for me to update this blog.