Crystal structure of the ectoine hydroxylase, a snapshot of the active site

Journal of Biological Chemistry

Volumn 289, Issue 43, 2014, Pages 29570-29583

  Höppner, Astrid ^a   Widderich, Nils ^b,c,d   Lenders, Michael ^a   Bremer, Erhard ^b   Smits, Sander H J ^a  

^a HEINRICH HEINE UNIVERSITY   (Germany)

^b PHILIPPS UNIVERSITY MARBURG   (Germany)

^c MAX PLANCK INSTITUTE FOR TERRESTRIAL MICROBIOLOGY   (Germany)

^d and Molecular Microbiology   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSTS; HYDROXYLATION; IRON; IRON COMPOUNDS; LIGANDS; PROTEINS;

2-OXOGLUTARATE; 2-OXOGLUTARATE-DEPENDENT DIOXYGENASE; CHEMICAL CHAPERONE; COMPATIBLE SOLUTES; CRYSTALLOGRAPHIC ANALYSIS; ENZYMATIC REACTION; OSMOTIC STRESS; RECEPTOR PROTEINS;

CRYSTAL STRUCTURE;

2 OXOGLUTARIC ACID; 5 HYDROXYECTOINE; ECTOINE; ECTOINE HYDROXYLASE; IRON; OXYGENASE; UNCLASSIFIED DRUG; ALPHA-KETOGLUTARIC ACID; BACTERIAL PROTEIN; DIAMINO ACID; HYBRID PROTEIN; HYDROXYECTOINE; MIXED FUNCTION OXIDASE; MUTANT PROTEIN; SOLUTION AND SOLUBILITY;

ARTICLE; BINDING AFFINITY; CATALYST; CHEMICAL REACTION; COMPLEX FORMATION; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME STRUCTURE; HYDROXYLATION; MICROBACTERIUM; NONHUMAN; NUCLEOTIDE SEQUENCE; SPHINGOPYXIS ALASKENSIS; AMINO ACID SEQUENCE; BACTERIA; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GEL CHROMATOGRAPHY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; METABOLISM; MOLECULAR GENETICS; MUTAGENESIS; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT; SOLUTION AND SOLUBILITY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; AMINO ACIDS, DIAMINO; BACTERIA; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CHROMATOGRAPHY, GEL; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CRYSTALLOGRAPHY, X-RAY; IRON; KETOGLUTARIC ACIDS; MIXED FUNCTION OXYGENASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; MUTANT PROTEINS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SOLUTIONS;

EID: 84908432708     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.576769     Document Type: Article

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