2FYO

Crystal structure of rat carnitine palmitoyltransferase 2 in space group P43212

PDB DOI: https://doi.org/10.2210/pdb2FYO/pdb

Classification: TRANSFERASE
Organism(s): Rattus norvegicus
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2006-02-08 Released: 2007-02-08
Deposition Author(s): Rufer, A.C., Thoma, R., Benz, J., Stihle, M., Gsell, B., De Roo, E., Banner, D.W., Mueller, F., Chomienne, O., Hennig, M.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.00 Å
R-Value Free: 0.235
R-Value Work: 0.179
R-Value Observed: 0.182

wwPDB Validation 3D Report Full Report

This is version 1.3 of the entry. See complete history.

Literature

The crystal structure of carnitine palmitoyltransferase 2 and implications for diabetes treatment

Rufer, A.C., Thoma, R., Benz, J., Stihle, M., Gsell, B., De Roo, E., Banner, D.W., Mueller, F., Chomienne, O., Hennig, M.

(2006) Structure 14: 713-723

PubMed: 16615901 Search on PubMed
DOI: https://doi.org/10.1016/j.str.2006.03.002
Primary Citation of Related Structures:
2DEB, 2FW3, 2FYO

PubMed Abstract:
Carnitine palmitoyltransferases (CPTs) are part of the enzymatic system that imports fatty acids into mitochondria. The crystal structure of rat CPT-2 by Rufer et al. (2006) (this issue of Structure) reveals a Y-shaped tunnel for binding the CoA and acyl-carnitine substrates and a hydrophobic insert mediating membrane association.

Macromolecule Content

Total Structure Weight: 74.13 kDa
Atom Count: 5,501
Modelled Residue Count: 625
Deposited Residue Count: 653
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Carnitine O-palmitoyltransferase II, mitochondrial	A	653	Rattus norvegicus	Mutation(s): 12 EC: 2.3.1.21
UniProt
Find proteins for P18886 (Rattus norvegicus) Explore P18886 Go to UniProtKB: P18886
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P18886
Sequence Annotations Expand
Reference Sequence

Small Molecules

Modified Residues 1 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
MSE Query on MSE	A	L-PEPTIDE LINKING	C₅ H₁₁ N O₂ Se		MET

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.00 Å
R-Value Free: 0.235
R-Value Work: 0.179
R-Value Observed: 0.182
Space Group: P 4₃ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 67.55	α = 90
b = 67.55	β = 90
c = 307.28	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
MAR345	data collection
XDS	data scaling
PHASER	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2007-02-08

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2007-02-08
Type: Initial release
Version 1.1: 2008-05-01
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2017-10-18
Changes: Refinement description

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.