1bjp: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1bjp.jpg|left|200px]]
{{Seed}}
[[Image:1bjp.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1bjp|  PDB=1bjp  |  SCENE=  }}  
{{STRUCTURE_1bjp|  PDB=1bjp  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF 4-OXALOCROTONATE TAUTOMERASE INACTIVATED BY 2-OXO-3-PENTYNOATE AT 2.4 ANGSTROMS RESOLUTION'''
===CRYSTAL STRUCTURE OF 4-OXALOCROTONATE TAUTOMERASE INACTIVATED BY 2-OXO-3-PENTYNOATE AT 2.4 ANGSTROMS RESOLUTION===




==Overview==
<!--
The crystal structure of 4-oxalocrotonate tautomerase (4-OT) inactivated by the active site-directed irreversible inhibitor 2-oxo-3-pentynoate (2-OP) has been determined to 2.4 A resolution. The structure of the enzyme covalently modified at Pro-1 by the resulting 2-oxo-3-pentenoate adduct is nearly superimposable on that of the free enzyme and confirms that the active site is located in a hydrophobic region surrounding Pro-1. Both structures can be described as a trimer of dimers where each dimer consists of a four-stranded beta-sheet with two antiparallel alpha-helices on one side. Examination of the structure also reveals noncovalent interactions between the adduct and two residues in the active site. The epsilon and eta nitrogens of the guanidinium side chain of Arg-39" from a neighboring dimer interact respectively with the C-2 carbonyl oxygen and one C-1 carboxylate oxygen of the adduct while the side chain of Arg-61' from the same dimer as the modified Pro-1 interacts with the C-1 carboxylate group in a bidentate fashion. An additional interaction to the 2-oxo group of the adduct is provided by one of the two ordered water molecules within the active site region. These interactions coupled with the observation that 2-oxo-3-butynoate is a more potent irreversible inhibitor of 4-oxalocrotonate tautomerase than is 2-OP suggest that Arg-39" and the ordered water molecule polarize the carbonyl group of 2-OP which facilitates a Michael reaction between Pro-1 and the acetylene compound. On the basis of the crystal structure, a mechanism for the enzyme-catalyzed reaction is proposed.
The line below this paragraph, {{ABSTRACT_PUBMED_9778344}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9778344 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_9778344}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Microbial biodegradation]]
[[Category: Microbial biodegradation]]
[[Category: Tautomerase]]
[[Category: Tautomerase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:36:17 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:16:22 2008''

Revision as of 16:16, 30 June 2008

File:1bjp.png

Template:STRUCTURE 1bjp

CRYSTAL STRUCTURE OF 4-OXALOCROTONATE TAUTOMERASE INACTIVATED BY 2-OXO-3-PENTYNOATE AT 2.4 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 9778344

About this Structure

1BJP is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.

Reference

Crystal structure of 4-oxalocrotonate tautomerase inactivated by 2-oxo-3-pentynoate at 2.4 A resolution: analysis and implications for the mechanism of inactivation and catalysis., Taylor AB, Czerwinski RM, Johnson WH Jr, Whitman CP, Hackert ML, Biochemistry. 1998 Oct 20;37(42):14692-700. PMID:9778344

Page seeded by OCA on Mon Jun 30 19:16:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1bjp&oldid=578098"