4Q31: The Crystal Structure Of Cystathione Gamma Lyase (cale6) From Micromonospora Echinospora

Citation:
Abstract
CalE6 from Micromonospora echinospora is a (pyridoxal 5' phosphate) PLP-dependent methionine gamma-lyase involved in the biosynthesis of calicheamicins. We report the crystal structure of a CalE6 2-(N-morpholino)ethanesulfonic acid complex showing ligand-induced rotation of Tyr100, which stacks with PLP, resembling the corresponding tyrosine rotation of true catalytic intermediates of CalE6 homologs. Elastic network modeling and crystallographic ensemble refinement reveal mobility of the N-terminal loop, which involves both tetrameric assembly and PLP binding. Modeling and comparative structural analysis of PLP-dependent enzymes involved in Cys/Met metabolism shine light on the functional implications of the intrinsic dynamic properties of CalE6 in catalysis and holoenzyme maturation.
PDB ID: 4Q31Download
MMDB ID: 119644
PDB Deposition Date: 2014/4/10
Updated in MMDB: 2014/05
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 4Q31: tetrameric; determined by author and by software (PISA)
Molecular Components in 4Q31
Label Count Molecule
Proteins (4 molecules)
4
Cystathione Gamma Lyase Cale6
Molecule annotation
Chemicals (28 molecules)
1
4
2
7
3
15
4
2
* Click molecule labels to explore molecular sequence information.

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