PDBsum entry 1bpv

Connectin

PDB id: 1bpv

Contents

Protein chain

104 a.a. *

* Residue conservation analysis

PDB id:

1bpv

Name:

Connectin

Title:

Titin module a71 from human cardiac muscle, nmr, 50 structures

Structure:

Titin. Chain: a. Fragment: 71 th domain from the a-band. Synonym: a71, connectin. Engineered: yes. Mutation: yes

Source:

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

NMR struc:

50 models

Authors:

C.Muhle-Goll,A.Pastore,M.Nilges

Key ref:

C.M.Goll et al. (1998). The three-dimensional structure of a type I module from titin: a prototype of intracellular fibronectin type III domains. Structure, 6, 1291-1302. PubMed id: 9782056 DOI: 10.1016/S0969-2126(98)00129-4

Date:

11-Aug-98 Release date: 12-Aug-99

Protein chain

Q8WZ42  (TITIN_HUMAN) -  Titin from Homo sapiens

Seq: 34350 a.a.

Struc: 104 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.2.7.11.1 - non-specific serine/threonine protein kinase.
• 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⁺

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

reference

DOI no: 10.1016/S0969-2126(98)00129-4

Structure 6:1291-1302 (1998)

PubMed id: 9782056

The three-dimensional structure of a type I module from titin: a prototype of intracellular fibronectin type III domains.

C.M.Goll, A.Pastore, M.Nilges.

ABSTRACT

BACKGROUND: Titin is a huge protein ( approximately 3 MDa) that is present in the contractile unit (sarcomere) of striated muscle and has a key role in muscle assembly and elasticity. Titin is mainly composed of two types of module (type I and II). Type I modules are found exclusively in the region of titin localised in the A band, where they are arranged in a super-repeat pattern that correlates with the ultrastructure of the thick filament. No structure of a titin type I module has been reported so far. RESULTS: We have determined the structure of a representative type I module, A71, using nuclear magnetic resonance (NMR) spectroscopy. The structure has the predicted fibronectin type III fold. Titin-specific conserved residues are either located at the putative module-module interfaces or along one side of the protein surface. Several proline residues that contribute to two stretches in a polyproline II helix conformation are solvent-exposed and line up as a continuous ribbon extending over more than two-thirds of the module surface. Homology models of the type I module N-terminal to A71 (A70) and the double module A70-A71 were used to discuss possible intermodule interactions and their role in module-module orientation. CONCLUSIONS: As residues at the module-module interfaces are highly conserved, we speculate that similar interactions govern all of the interfaces between type I modules in titin. This conservation would lead to a regular multiple array of similar surface structures. Such an arrangement would allow arrays of contiguous type I modules to expose multiple proline stretches in a highly regular way and these may act as binding sites for other thick filament proteins.

Selected figure(s)

Figure 6.
Figure 6. The solvent-exposed surface of A71. The surface is displayed as white dots surrounding the CPK structure of A71. Exposed proline sidechains (coloured in yellow) and the adjacent hydrophobic patch of isoleucine residues (coloured in light green) are shown in solid surface representation.

The above figure is reprinted by permission from Cell Press: Structure (1998, 6, 1291-1302) copyright 1998.

Figure was selected by an automated process.