1T8K

Crystal Structure of apo acyl carrier protein from E. coli

Summary for 1T8K

• Entry DOI: 10.2210/pdb1t8k/pdb
• Descriptor: Acyl carrier protein, ZINC ION, IMIDAZOLE, ... (4 entities in total)
• Functional Keywords: acp, lipid transport
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A6A8
• Total number of polymer chains: 1
• Total formula weight: 9582.86

Authors

Qiu, X.,Janson, C.A. (deposition date: 2004-05-13, release date: 2004-09-07, Last modification date: 2024-02-14)

Primary citation

Qiu, X.,Janson, C.A.
Structure of apo acyl carrier protein and a proposal to engineer protein crystallization through metal ions.
Acta Crystallogr.,Sect.D, 60:1545-1554, 2004

PubMed Abstract: A topic of current interest is engineering surface mutations in order to improve the success rate of protein crystallization. This report explores the possibility of using metal-ion-mediated crystal-packing interactions to facilitate rational design. Escherichia coli apo acyl carrier protein was chosen as a test case because of its high content of negatively charged carboxylates suitable for metal binding with moderate affinity. The protein was successfully crystallized in the presence of zinc ions. The crystal structure was determined to 1.1 A resolution with MAD phasing using anomalous signals from the co-crystallized Zn(2+) ions. The case study suggested an integrated strategy for crystallization and structure solution of proteins via engineering surface Asp and Glu mutants, crystallizing them in the presence of metal ions such as Zn(2+) and solving the structures using anomalous signals.

PubMed: 15333924
DOI: 10.1107/S0907444904015422

Experimental method

X-RAY DIFFRACTION (1.1 Å)