Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase.

Nature structural biology ·Vol. 4 ·No. 1 ·1997-01-00 ·Pages 36-9

Blom N, Sygusch J

Abstract

The structure of fructose 1,6-bisphosphate aldolase shows three distinct modes of product binding that are correlated to the disposition of the C-terminal region and depicts a possible trajectory for product exchange. The structure also indicates binding preference for monobasic triose phosphates.

MeSH Terms

Animals Binding Sites Fructose-Bisphosphate Aldolase/chemistry,metabolism Protein Binding Protein Conformation Rabbits

Chemicals

Fructose-Bisphosphate Aldolase

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Blom N

Sygusch J

Article Info

Journal

Nature structural biology

Abbr.

Nat Struct Biol

ISSN

1072-8368

DOI

10.1038/nsb0197-36

Published

1997-01-00

Pages

36-9

Language

English

Region

United States

NLM ID

9421566

Subset

External Links

PubMed source DOI: 10.1038/nsb0197-36

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Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase.

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