PDBsum entry 6h4l

Structural protein

PDB id

6h4l

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Contents

			Protein chain

					96 a.a.

			Metals

					_CL ×3


					_ZN

			Waters ×195

PDB id:

6h4l

Links

Name:

Structural protein

Title:

Structure of titin m4 trigonal form

Structure:

Titin. Chain: a. Synonym: connectin,rhabdomyosarcoma antigen mu-rms-40.14. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ttn. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008

Resolution:

1.60Å

R-factor:

0.209

R-free:

0.221

Authors:

F.Sauer,M.Wilmanns

Key ref:

S.D.Chatziefthimiou et al. (2019). Structural diversity in the atomic resolution 3D fingerprint of the titin M-band segment. PLoS One, 14, e0226693. PubMed id: 31856237 DOI: 10.1371/journal.pone.0226693

Date:

21-Jul-18

Release date:

07-Aug-19

PROCHECK

	Headers

	References

Protein chain

Q8WZ42 (TITIN_HUMAN) - Titin from Homo sapiens

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Seq: Struc:					34350 a.a. 96 a.a.

Key:

Secondary structure



		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

DOI no: 10.1371/journal.pone.0226693	PLoS One 14:e0226693 (2019)
PubMed id: 31856237

Structural diversity in the atomic resolution 3D fingerprint of the titin M-band segment.
S.D.Chatziefthimiou, P.Hornburg, F.Sauer, S.Mueller, D.Ugurlar, E.R.Xu, M.Wilmanns.

ABSTRACT

In striated muscles, molecular filaments are largely composed of long protein chains with extensive arrays of identically folded domains, referred to as "beads-on-a-string". It remains a largely unresolved question how these domains have developed a unique molecular profile such that each carries out a distinct function without false-positive readout. This study focuses on the M-band segment of the sarcomeric protein titin, which comprises ten identically folded immunoglobulin domains. Comparative analysis of high-resolution structures of six of these domains ‒ M1, M3, M4, M5, M7, and M10 ‒ reveals considerable structural diversity within three distinct loops and a non-conserved pattern of exposed cysteines. Our data allow to structurally interpreting distinct pathological readouts that result from titinopathy-associated variants. Our findings support general principles that could be used to identify individual structural/functional profiles of hundreds of identically folded protein domains within the sarcomere and other densely crowded cellular environments.