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3SI9

Crystal structure of Dihydrodipicolinate Synthase from Bartonella Henselae

Summary for 3SI9
Entry DOI10.2210/pdb3si9/pdb
DescriptorDihydrodipicolinate synthase, 1,2-ETHANEDIOL (3 entities in total)
Functional Keywordsstructural genomics, seattle structural genomics center for infectious disease, ssgcid, tim barrel, lyase
Biological sourceBartonella henselae
Cellular locationCytoplasm : Q6G468
Total number of polymer chains4
Total formula weight135801.74
Authors
Seattle Structural Genomics Center for Infectious Disease (SSGCID),Staker, B.L.,Abendroth, J.,Sankaran, B. (deposition date: 2011-06-17, release date: 2011-06-29, Last modification date: 2023-09-13)
Primary citationNaqvi, K.F.,Staker, B.L.,Dobson, R.C.,Serbzhinskiy, D.,Sankaran, B.,Myler, P.J.,Hudson, A.O.
Cloning, expression, purification, crystallization and X-ray diffraction analysis of dihydrodipicolinate synthase from the human pathogenic bacterium Bartonella henselae strain Houston-1 at 2.1 angstrom resolution.
Acta Crystallogr F Struct Biol Commun, 72:2-9, 2016
Cited by
PubMed Abstract: The enzyme dihydrodipicolinate synthase catalyzes the committed step in the synthesis of diaminopimelate and lysine to facilitate peptidoglycan and protein synthesis. Dihydrodipicolinate synthase catalyzes the condensation of L-aspartate 4-semialdehyde and pyruvate to synthesize L-2,3-dihydrodipicolinate. Here, the cloning, expression, purification, crystallization and X-ray diffraction analysis of dihydrodipicolinate synthase from the pathogenic bacterium Bartonella henselae, the causative bacterium of cat-scratch disease, are presented. Protein crystals were grown in conditions consisting of 20%(w/v) PEG 4000, 100 mM sodium citrate tribasic pH 5.5 and were shown to diffract to ∼2.10 Å resolution. They belonged to space group P212121, with unit-cell parameters a = 79.96, b = 106.33, c = 136.25 Å. The final R values were Rr.i.m. = 0.098, Rwork = 0.183, Rfree = 0.233.
PubMed: 26750477
DOI: 10.1107/S2053230X15023213
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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数据于2025-06-25公开中

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