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Chlamydia trachomatis glyceraldehyde 3-phosphate dehydrogenase: Enzyme kinetics, high-resolution crystal structure, and plasminogen binding.
- Source :
-
Protein science : a publication of the Protein Society [Protein Sci] 2020 Dec; Vol. 29 (12), pp. 2446-2458. Date of Electronic Publication: 2020 Oct 30. - Publication Year :
- 2020
-
Abstract
- Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is an evolutionarily conserved essential enzyme in the glycolytic pathway. GAPDH is also involved in a wide spectrum of non-catalytic cellular 'moonlighting' functions. Bacterial surface-associated GAPDHs engage in many host interactions that aid in colonization, pathogenesis, and virulence. We have structurally and functionally characterized the recombinant GAPDH of the obligate intracellular bacteria Chlamydia trachomatis, the leading cause of sexually transmitted bacterial and ocular infections. Contrary to earlier speculations, recent data confirm the presence of glucose-catabolizing enzymes including GAPDH in both stages of the biphasic life cycle of the bacterium. The high-resolution crystal structure described here provides a close-up view of the enzyme's active site and surface topology and reveals two chemically modified cysteine residues. Moreover, we show for the first time that purified C. trachomatis GAPDH binds to human plasminogen and plasmin. Based on the versatility of GAPDH's functions, data presented here emphasize the need for investigating the Chlamydiae GAPDH's involvement in biological functions beyond energy metabolism.<br /> (© 2020 The Protein Society.)
- Subjects :
- Bacterial Proteins metabolism
Crystallography, X-Ray
Glyceraldehyde-3-Phosphate Dehydrogenases metabolism
Plasminogen metabolism
Protein Binding
Bacterial Proteins chemistry
Chlamydia trachomatis enzymology
Glyceraldehyde-3-Phosphate Dehydrogenases chemistry
Models, Molecular
Plasminogen chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1469-896X
- Volume :
- 29
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Protein science : a publication of the Protein Society
- Publication Type :
- Academic Journal
- Accession number :
- 33058314
- Full Text :
- https://doi.org/10.1002/pro.3975