PDBsum entry 1waa

Metal binding protein

PDB id

1waa

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Contents

			Protein chains

					92 a.a. *


					92 a.a. *


					93 a.a. *

			Metals

					_ZN ×24

			Waters ×480

* Residue conservation analysis

PDB id:

1waa

Links

Name:

Metal binding protein

Title:

Ig27 protein domain

Structure:

Titin. Chain: a, b, c, d. Fragment: ig domain, residues 12801-12889. Synonym: i27 domain from titin, heart isoform n2-b. Engineered: yes. Titin. Chain: e. Fragment: ig domain, residues 12801-12889. Synonym: i27 domain from titin, heart isoform n2-b.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Organ: heart. Tissue: muscle. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562

Biol. unit:

Hexamer (from PDB file)

Resolution:

1.80Å

R-factor:

0.211

R-free:

0.268

Authors:

M.C.Vega,L.Valencia,P.Zou,M.Wilmanns

Key ref:

W.Stacklies et al. (2009). Mechanical network in titin immunoglobulin from force distribution analysis. Plos Comput Biol, 5, e1000306. PubMed id: 19282960

Date:

25-Oct-04

Release date:

05-Jul-06

PROCHECK

	Headers

	References

Protein chains

Q8WZ42 (TITIN_HUMAN) - Titin from Homo sapiens

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Seq: Struc:					34350 a.a. 92 a.a.*

Protein chain

Q8WZ42 (TITIN_HUMAN) - Titin from Homo sapiens

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Seq: Struc:					34350 a.a. 92 a.a.*

Protein chain

Q8WZ42 (TITIN_HUMAN) - Titin from Homo sapiens

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Seq: Struc:					34350 a.a. 93 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 22 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

Chains A, B, C, D, E, F: 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

	Plos Comput Biol 5:e1000306 (2009)
PubMed id: 19282960

Mechanical network in titin immunoglobulin from force distribution analysis.
W.Stacklies, M.C.Vega, M.Wilmanns, F.Gräter.

ABSTRACT

The role of mechanical force in cellular processes is increasingly revealed by single molecule experiments and simulations of force-induced transitions in proteins. How the applied force propagates within proteins determines their mechanical behavior yet remains largely unknown. We present a new method based on molecular dynamics simulations to disclose the distribution of strain in protein structures, here for the newly determined high-resolution crystal structure of I27, a titin immunoglobulin (IG) domain. We obtain a sparse, spatially connected, and highly anisotropic mechanical network. This allows us to detect load-bearing motifs composed of interstrand hydrogen bonds and hydrophobic core interactions, including parts distal to the site to which force was applied. The role of the force distribution pattern for mechanical stability is tested by in silico unfolding of I27 mutants. We then compare the observed force pattern to the sparse network of coevolved residues found in this family. We find a remarkable overlap, suggesting the force distribution to reflect constraints for the evolutionary design of mechanical resistance in the IG family. The force distribution analysis provides a molecular interpretation of coevolution and opens the road to the study of the mechanism of signal propagation in proteins in general.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20542682

N.Crampton, and D.J.Brockwell (2010).
Unravelling the design principles for single protein mechanical strength.

Curr Opin Struct Biol, 20, 508-517.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.