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2ats
From Proteopedia
| 2ats, resolution 1.90Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||||
| Activity: | Dihydrodipicolinate synthase, with EC number 4.2.1.52 | ||||||||
| Domains: | DHDPS, PRK03170 | ||||||||
| Related: | 1dhp, 1o5k, 1s5t, 1s5v, 1s5w, 1yxd | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Dihydrodipicolinate synthase co-crystallised with (S)-lysine
Cartoon representation of YagE showing the 2-fold symmetry axes between monomers. Chains A, B, C, and D are colored cyan, lime, magenta, and yellow, respectively (2v9d). of YagE (cyan) with (1nal, yellow), (1w3i, magenta), (1xky, lime), and (2ats, blue) monomers. Although YagE possesses only 23, 24, and 27% sequence identity with EcNAL, SsKDGA, EcDHDPS, respectively, their monomeric structures are all very similar. Superposition of active site residues of YagE with (magenta, 1w3i), (blue, 2ats), and (yellow, 1nal), residues are labeled according to the corresponding PDB structures. Members of the NAL protein subfamily have very similar active sites and a single amino acid substitution can significantly change their function. For example, NAL (1nal) gets DHDPS activity by substitution of a (orange) to (blue) at position 142. The possible active site region of YagE demonstrates closest sequence similarity to the active site of KDG aldolase of SsKDGA (1w3i) and NAL of EcNAL (1nal) (yellow), suggesting that this protein can perform either of these functions. Although the active site of EcDHDPS (1xky) and BaDHDPS (2ats) shows similarities, the important residue that differentiates between NAL and DHDPS, namely Leu142 (in 1nal), is also present in YagE (labeled cyan) at that particular position suggesting that YagE performs a NAL-related function rather than DHDPS-related one.
About this Structure
2ATS is a 2 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
References
The co-crystallisation of (S)-lysine-bound dihydrodipicolinate synthase from E. coli indicates that domain movements are not responsible for (S)-lysine inhibition Devenish, S.R.A., Dobson, R.C.J., Jameson, G.B., Gerrard, J.A. Journal: To be published. Not in PubMed
- Manicka S, Peleg Y, Unger T, Albeck S, Dym O, Greenblatt HM, Bourenkov G, Lamzin V, Krishnaswamy S, Sussman JL. Crystal structure of YagE, a putative DHDPS-like protein from Escherichia coli K12. Proteins. 2008 Jun;71(4):2102-8. PMID:18361457 doi:10.1002/prot.22023
Page seeded by OCA on Mon Feb 16 12:54:59 2009
