1DD8

CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I FROM ESCHERICHIA COLI

PDB DOI: https://doi.org/10.2210/pdb1DD8/pdb

Classification: TRANSFERASE
Organism(s): Escherichia coli
Mutation(s): No

Deposited: 1999-11-09 Released: 1999-11-18
Deposition Author(s): Olsen, J.G., Kadziola, A., von Wettstein-Knowles, P., Siggaard-Andersen, M., Lindquist, Y., Larsen, S.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Free: 0.219
R-Value Work: 0.188

wwPDB Validation 3D Report Full Report

This is version 1.4 of the entry. See complete history.

Literature

The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I.

Olsen, J.G., Kadziola, A., von Wettstein-Knowles, P., Siggaard-Andersen, M., Lindquist, Y., Larsen, S.

(1999) FEBS Lett 460: 46-52

PubMed: 10571059 Search on PubMed
DOI: https://doi.org/10.1016/s0014-5793(99)01303-4
Primary Citation of Related Structures:
1DD8

PubMed Abstract:
The crystal structure of the fatty acid elongating enzyme beta-ketoacyl [acyl carrier protein] synthase I (KAS I) from Escherichia coli has been determined to 2.3 A resolution by molecular replacement using the recently solved crystal structure of KAS II as a search model. The crystal contains two independent dimers in the asymmetric unit. KAS I assumes the thiolase alpha(beta)alpha(beta)alpha fold. Electrostatic potential distribution reveals an acyl carrier protein docking site and a presumed substrate binding pocket was detected extending the active site. Both subunits contribute to each substrate binding site in the dimer.

Organizational Affiliation

Centre for Crystallographic Studies, University of Copenhagen, Denmark.

Macromolecule Content

Total Structure Weight: 170.74 kDa
Atom Count: 12,440
Modelled Residue Count: 1,624
Deposited Residue Count: 1,624
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
BETA-KETOACYL [ACYL CARRIER PROTEIN] SYNTHASE I	A, B, C, D	406	Escherichia coli	Mutation(s): 0 EC: 2.3.1.41
UniProt
Find proteins for P0A953 (Escherichia coli (strain K12)) Explore P0A953 Go to UniProtKB: P0A953
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P0A953
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Free: 0.219
R-Value Work: 0.188
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 59.62	α = 90
b = 142.71	β = 90
c = 213.46	γ = 90

Software Package:

Software Name	Purpose
X-PLOR	model building
X-PLOR	refinement
DENZO	data reduction
SCALEPACK	data scaling
X-PLOR	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 1999-11-18

Deposition Author(s):

von Wettstein-Knowles, P.

Siggaard-Andersen, M.

Revision History (Full details and data files)

Version 1.0: 1999-11-18
Type: Initial release
Version 1.1: 2008-04-27
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2018-01-31
Changes: Experimental preparation
Version 1.4: 2024-02-07
Changes: Data collection, Database references

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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 R01GM157729.