1eb4 | pdb_00001eb4

Histidine Ammonia-Lyase (HAL) Mutant F329A from Pseudomonas putida

spinqualitylabelsall models 1eb4, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1eb4 is a 1 chain structure with sequence from Pseudomonas putida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: GOL, MDO, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HUTH_PSEPU Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Histidine ammonia-lyase requires a 4-methylidene-imidazole-5-one group (MIO) that is produced autocatalytically by a cyclization and dehydration step in a 3-residue loop of the polypeptide. The crystal structures of three mutants have been established. Two mutants were inactive and failed to form MIO, but remained unchanged elsewhere. The third mutant showed very low activity and formed MIO, although it differed from an MIO-less mutant only by an additional 329-C(beta) atom. This atom forms one constraint during MIO formation, the other being the strongly connected Asp145. An exploration of the conformational space of the MIO-forming loop showed that the cyclization is probably enforced by a mechanic compression in a late stage of chain folding and is catalyzed by a well-connected internal water molecule. The cyclization of the respective 3-residue loop of green fluorescent protein is likely to occur in a similar reaction. Autocatalytic peptide cyclization during chain folding of histidine ammonia-lyase.,Baedeker M, Schulz GE Structure. 2002 Jan;10(1):61-7. PMID:11796111 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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