PDBsum entry 2rq8

Transferase

PDB id

2rq8

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Contents

			Protein chain

					98 a.a. *

* Residue conservation analysis

PDB id:

2rq8

Links
- PDBe
- RCSB
- MMDB
- JenaLib
- Proteopedia
- CATH
- SCOP
- PDBSWS
- ProSAT

Name:

Transferase

Title:

Solution nmr structure of titin i27 domain mutant

Structure:

Titin. Chain: a. Fragment: unp residues 12677-12765. Synonym: connectin, rhabdomyosarcoma antigen mu-rms-40.14. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ttn. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

K.Yagawa,T.Oguro,T.Momose,S.Kawano,T.Sato,T.Endo

Key ref:

K.Yagawa et al. (2010). Structural basis for unfolding pathway-dependent stability of proteins: vectorial unfolding versus global unfolding. Protein Sci, 19, 693-702. PubMed id: 20095049

Date:

05-Mar-09

Release date:

02-Feb-10

PROCHECK

	Headers

	References

Protein chain

Q8WZ42 (TITIN_HUMAN) - Titin from Homo sapiens

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Seq: Struc:					34350 a.a. 98 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 13 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

E.C.2.7.11.1 - non-specific serine/threonine protein kinase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

1.	L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
2.	L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

L-seryl-[protein]	+	ATP	=	O-phospho-L-seryl-[protein]	+	ADP	+	H(+)

L-threonyl-[protein]	+	ATP	=	O-phospho-L-threonyl-[protein]	+	ADP	+	H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

	Protein Sci 19:693-702 (2010)
PubMed id: 20095049

Structural basis for unfolding pathway-dependent stability of proteins: vectorial unfolding versus global unfolding.
K.Yagawa, K.Yamano, T.Oguro, M.Maeda, T.Sato, T.Momose, S.Kawano, T.Endo.

ABSTRACT

Point mutations in proteins can have different effects on protein stability depending on the mechanism of unfolding. In the most interesting case of I27, the Ig-like module of the muscle protein titin, one point mutation (Y9P) yields opposite effects on protein stability during denaturant-induced "global unfolding" versus "vectorial unfolding" by mechanical pulling force or cellular unfolding systems. Here, we assessed the reason for the different effects of the Y9P mutation of I27 on the overall molecular stability and N-terminal unraveling by NMR. We found that the Y9P mutation causes a conformational change that is transmitted through beta-sheet structures to reach the central hydrophobic core in the interior and alters its accessibility to bulk solvent, which leads to destabilization of the hydrophobic core. On the other hand, the Y9P mutation causes a bend in the backbone structure, which leads to the formation of a more stable N-terminal structure probably through enhanced hydrophobic interactions.