Substrate binding induces domain movements in orotidine 5′-monophosphate decarboxylase

Journal of Molecular Biology

Volumn 318, Issue 4, 2002, Pages 1019-1029

  Harris, Pernille ^a   Poulsen, Jens Christian Navarro ^a   Jensen, Kaj Frank ^b   Larsen, Sine ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

Catalysis; Domain movements; Orotidine 5 monophosphate decarboxylase; Substrate binding; Twinning

Indexed keywords

1 (5' PHOSPHO BETA DEXTRO RIBOFURANOSYL)BARBITURIC ACID; BARBITURIC ACID DERIVATIVE; BLOCKING AGENT; OROTIDINE 5' PHOSPHATE DECARBOXYLASE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; METHANOBACTERIUM THERMOAUTOTROPHICUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; SACCHAROMYCES CEREVISIAE; STRUCTURE ANALYSIS;

ESCHERICHIA COLI; METHANOBACTERIUM; METHANOTHERMOBACTER THERMAUTOTROPHICUS; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 0036040211     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00200-0     Document Type: Article

References (30)

1. A proficient enzyme
2. Model chemistry for a covalent mechanism of action of orotidine 5′-phosphate decarboxylase
3. Mechanism of decarboxylation of 1,3-dimethylorotic acid. A model for orotidine 5′-phosphate decarboxylase
4. A proficient enzyme revisited: The predicted mechanism for orotidine monophosphate decarboxylase
5. Structural basis for the catalytic mechanism of a proficient enzyme: Orotidine 5′-monophosphate decarboxylase
6. The crystal structure and mechanism of orotidine 5′-monophosphate decarboxylase
7. Electrostatic stress in catalysis: Structure and mechanism of the enzyme orotidine monophosphate decarboxylase
8. Anatomy of a proficient enzyme: The structure of orotidine 5′-monophosphate decarboxylase in the presence and absence of a potential transition state analog
9. The mechanism of orotidine 5′-monophosphate decarboxylase: Catalysis by destabilization of the substrate
10. The buzz about a remarkable enzyme
11. Contribution of enzyme-phosphoribosyl contacts to catalysis by orotidine 5′-phosphate decarboxylase
12. Dissecting a charged network at the active site of orotidine-5′-phosphate decarboxylase
13. Role of enzyme-ribofuranosyl contacts in the ground state and transition state for orotidine 5′-phosphate decarboxylase: A role for substrate destabilization
14. AMoRe: An automated molecular replacement program package
15. Crystallography and nmr system: A new software suite for macromolecular structure determination
16. Protein domain movements: Detection of rigid domains and visualization of hinges in comparisons of atomic coordinates
17. Systematic analysis of domain motions in proteins from conformational change; new results on citrate synthase and t4 lysozyme
18. Yeast orotidine-5′-phosphate decarboxylase: Steady-state and pre-steady-state analysis of the kinetic mechanism of substrate decarboxylation
19. The structural basis for the remarkable catalytic proficiency of orotidine 5′-monophosphate decarboxylase
20. Evidence for a stepwise mechanism of omp decarboxylase
21. Selenomethionine substitution of orotidine-5′-monophosphate decarboxylase causes a change in crystal contacts and space group
22. Strategies in the crystallization of glycoproteins and protein complexes
23. Screening and optimization strategies for macromolecular crystal growth
24. Sparse matrix sampling: A screening method for crystallization of proteins
25. Protein crystallization using incomplete factorial experiments
26. Crystallization and preliminary X-ray analysis of maltose o-acetyltransferase
27. Simple statistics for intensity data from twinned specimens
28. Detecting and overcoming crystal twinning
29. Vmd - Visual molecular dynamics