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4LEM

Crystal structure of the Delta-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis

Summary for 4LEM
Entry DOI10.2210/pdb4lem/pdb
Related4IDM 4IDS 4IHI 4JDC
Descriptor1-pyrroline-5-carboxylate dehydrogenase, COBALAMIN, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsrossmann fold, dehydrogenase, oxidoreductase
Biological sourceMycobacterium tuberculosis
Total number of polymer chains6
Total formula weight372658.48
Authors
Lagautriere, T.,Bashiri, G.,Baker, E.N. (deposition date: 2013-06-26, release date: 2014-05-14, Last modification date: 2024-11-06)
Primary citationLagautriere, T.,Bashiri, G.,Baker, E.N.
Use of a "silver bullet" to resolve crystal lattice dislocation disorder: A cobalamin complex of Delta (1)-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis.
J.Struct.Biol., 189:153-157, 2015
Cited by
PubMed Abstract: The use of small molecules as "silver bullets" that can bind to generate crosslinks between protein molecules has been advanced as a powerful means of enhancing success in protein crystallization (McPherson and Cudney, 2006). We have explored this approach in attempts to overcome an order-disorder phenomenon that complicated the structural analysis of the enzyme Δ(1)-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis (P5CDH, Mtb-PruA). Using the Silver Bullets Bio screen, we obtained new crystal packing using cobalamin as a co-crystallization agent. This crystal form did not display the order-disorder phenomenon previously encountered. Solution of the crystal structure showed that cobalamin molecules are present in the crystal contacts. Although the cobalamin binding probably does not have physiological relevance, it reflects similarities in the nucleotide-binding region of Mtb-PruA, with the nucleotide loop of cobalamin sharing the binding site for the adenine moiety of NAD(+).
PubMed: 25557497
DOI: 10.1016/j.jsb.2014.12.007
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.27 Å)
Structure validation

246031

数据于2025-12-10公开中

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