2ggg: 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:2ggg.gif|left|200px]]
{{Seed}}
[[Image:2ggg.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ggg|  PDB=2ggg  |  SCENE=  }}  
{{STRUCTURE_2ggg|  PDB=2ggg  |  SCENE=  }}  


'''The mutant A68C-D72C of Deinococcus Radiodurans N-acylamino acid racemase'''
===The mutant A68C-D72C of Deinococcus Radiodurans N-acylamino acid racemase===




==Overview==
<!--  
N-Acylamino acid racemase (NAAAR) and N-carbamoyl-D-amino-acid amidohydrolase (D-NCAase) are important biocatalysts for producing enantiopure alpha-amino acids. NAAAR forms an octameric assembly and displays induced fit movements upon substrate binding, while D-NCAase is a tetramer that does not change conformation in the presence of a ligand. To investigate the effects of introducing potentially stabilizing S-S bridges in these different multimeric enzymes, cysteine residues predicted to form inter or intra-subunit disulfide bonds were introduced by site-directed mutagenesis. Inter-subunit S-S bonds were formed in two NAAAR variants (A68C-D72C and P60C-Y100C) and two d-NCAase variants (A302C and P295C-F304C). Intra-subunit S-S bonds were formed in two additional NAAAR variants (E149C-A182C and V265C). Crystal structures of NAAARs variants show limited deviations from the wild-type overall tertiary structure. An apo A68C-D72C subunit differs from the wild-type enzyme, in which it has an ordered lid loop, resembling ligand-bound NAAAR. The structures of A222C and A302C D-NCAases are nearly identical to the wild-type enzyme. All mutants with inter-subunit bridges had increases in thermostability. Compared with the wild-type enzyme, A68C-D72C NAAAR showed similar kcat/Km ratios, whereas mutant D-NCAases demonstrated increased kcat/Km ratios at high temperatures (A302C: 4.2-fold at 65 degrees C). Furthermore, molecular dynamic simulations reveal that A302C substantially sustains the fine-tuned catalytic site as temperature increases, achieving enhanced activity.
The line below this paragraph, {{ABSTRACT_PUBMED_16650857}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16650857 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_16650857}}


==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Deinococcus radioduran]]
[[Category: Deinococcus radioduran]]
[[Category: N-acylamino acid racemase]]
[[Category: N-acylamino acid racemase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:04:45 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:50:03 2008''

Revision as of 09:50, 28 July 2008

File:2ggg.png

Template:STRUCTURE 2ggg

The mutant A68C-D72C of Deinococcus Radiodurans N-acylamino acid racemase

Template:ABSTRACT PUBMED 16650857

About this Structure

2GGG is a Single protein structure of sequence from Deinococcus radiodurans. This structure supersedes the now removed PDB entries and 2ba6. Full crystallographic information is available from OCA.

Reference

Structure-stability-activity relationship in covalently cross-linked N-carbamoyl D-amino acid amidohydrolase and N-acylamino acid racemase., Chiu WC, You JY, Liu JS, Hsu SK, Hsu WH, Shih CH, Hwang JK, Wang WC, J Mol Biol. 2006 Jun 9;359(3):741-53. Epub 2006 Apr 18. PMID:16650857

Page seeded by OCA on Mon Jul 28 12:50:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2ggg&oldid=699298"