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The mechanism of aconitase: 1.8 A resolution crystal structure of the S642a:citrate complex.
Protein Sci. 1999 Dec; 8(12):2655-62.PS

Abstract

The crystal structure of the S642A mutant of mitochondrial aconitase (mAc) with citrate bound has been determined at 1.8 A resolution and 100 K to capture this binding mode of substrates to the native enzyme. The 2.0 A resolution, 100 K crystal structure of the S642A mutant with isocitrate binding provides a control, showing that the Ser --> Ala replacement does not alter the binding of substrates in the active site. The aconitase mechanism requires that the intermediate product, cis-aconitate, flip over by 180 degrees about the C alpha-C beta double bond. Only one of these two alternative modes of binding, that of the isocitrate mode, has been previously visualized. Now, however, the structure revealing the citrate mode of binding provides direct support for the proposed enzyme mechanism.

Authors+Show Affiliations

Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

10631981

Citation

Lloyd, S J., et al. "The Mechanism of Aconitase: 1.8 a Resolution Crystal Structure of the S642a:citrate Complex." Protein Science : a Publication of the Protein Society, vol. 8, no. 12, 1999, pp. 2655-62.
Lloyd SJ, Lauble H, Prasad GS, et al. The mechanism of aconitase: 1.8 A resolution crystal structure of the S642a:citrate complex. Protein Sci. 1999;8(12):2655-62.
Lloyd, S. J., Lauble, H., Prasad, G. S., & Stout, C. D. (1999). The mechanism of aconitase: 1.8 A resolution crystal structure of the S642a:citrate complex. Protein Science : a Publication of the Protein Society, 8(12), 2655-62.
Lloyd SJ, et al. The Mechanism of Aconitase: 1.8 a Resolution Crystal Structure of the S642a:citrate Complex. Protein Sci. 1999;8(12):2655-62. PubMed PMID: 10631981.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The mechanism of aconitase: 1.8 A resolution crystal structure of the S642a:citrate complex. AU - Lloyd,S J, AU - Lauble,H, AU - Prasad,G S, AU - Stout,C D, PY - 2000/1/13/pubmed PY - 2000/2/19/medline PY - 2000/1/13/entrez SP - 2655 EP - 62 JF - Protein science : a publication of the Protein Society JO - Protein Sci VL - 8 IS - 12 N2 - The crystal structure of the S642A mutant of mitochondrial aconitase (mAc) with citrate bound has been determined at 1.8 A resolution and 100 K to capture this binding mode of substrates to the native enzyme. The 2.0 A resolution, 100 K crystal structure of the S642A mutant with isocitrate binding provides a control, showing that the Ser --> Ala replacement does not alter the binding of substrates in the active site. The aconitase mechanism requires that the intermediate product, cis-aconitate, flip over by 180 degrees about the C alpha-C beta double bond. Only one of these two alternative modes of binding, that of the isocitrate mode, has been previously visualized. Now, however, the structure revealing the citrate mode of binding provides direct support for the proposed enzyme mechanism. SN - 0961-8368 UR - https://www.unboundmedicine.com/medline/citation/10631981/The_mechanism_of_aconitase:_1_8_A_resolution_crystal_structure_of_the_S642a:citrate_complex_ DB - PRIME DP - Unbound Medicine ER -