2d0d

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2d0d.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2d0d.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2d0d| PDB=2d0d | SCENE= }}
{{STRUCTURE_2d0d| PDB=2d0d | SCENE= }}
-
'''Crystal Structure of a Meta-cleavage Product Hydrolase (CumD) A129V Mutant'''
+
===Crystal Structure of a Meta-cleavage Product Hydrolase (CumD) A129V Mutant===
-
==Overview==
+
<!--
-
The meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) hydrolyzes 2-hydroxy-6-oxo-7-methylocta-2,4-dienoate (6-isopropyl HODA) in the cumene (isopropylbenzene) degradation pathway. To modulate the substrate specificity and catalytic efficiency of CumD toward substrates derived from monocyclic aromatic compounds, we constructed the CumD mutants, A129V, I199V, and V227I, as well as four types of double and triple mutants. Toward substrates with smaller side chains (e.g. 2-hydroxy-6-oxohepta-2,4-dienoate; 6-ethyl-HODA), the k(cat)/K(m) values of the single mutants were 4.2-11 fold higher than that of the wild type enzyme and 1.8-4.7 fold higher than that of the meta-cleavage product hydrolase from Pseudomonas putida F1 (TodF). The A129V mutant showed the highest k(cat)/K(m) value for 2-hydroxy-6-oxohepta-2,4-dienoate (6-ethyl-HODA). The crystal structure of the A129V mutant was determined at 1.65 A resolution, enabling location of the Ogamma atom of the Ser103 side chain. A chloride ion was bound to the oxyanion hole of the active site, and mutant enzymes at the residues forming this site were also examined. The k(cat) values of Ser34 mutants were decreased 2.9-65 fold, suggesting that the side chain of Ser34 supports catalysis by stabilizing the anionic oxygen of the proposed intermediate state (gem-diolate). This is the first crystal structure determination of CumD in an active form, with the Ser103 residue, one of the catalytically essential "triad", being intact.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16844437}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16844437 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16844437}}
==About this Structure==
==About this Structure==
Line 20: Line 24:
==Reference==
==Reference==
Improving the catalytic efficiency of a meta-cleavage product hydrolase (CumD) from Pseudomonas fluorescens IP01., Jun SY, Fushinobu S, Nojiri H, Omori T, Shoun H, Wakagi T, Biochim Biophys Acta. 2006 Jul;1764(7):1159-66. Epub 2006 Jun 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16844437 16844437]
Improving the catalytic efficiency of a meta-cleavage product hydrolase (CumD) from Pseudomonas fluorescens IP01., Jun SY, Fushinobu S, Nojiri H, Omori T, Shoun H, Wakagi T, Biochim Biophys Acta. 2006 Jul;1764(7):1159-66. Epub 2006 Jun 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16844437 16844437]
 +
 +
A series of crystal structures of a meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) complexed with various cleavage products., Fushinobu S, Jun SY, Hidaka M, Nojiri H, Yamane H, Shoun H, Omori T, Wakagi T, Biosci Biotechnol Biochem. 2005 Mar;69(3):491-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15784976 15784976]
 +
 +
Crystal structures of a meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) complexed with cleavage products., Fushinobu S, Saku T, Hidaka M, Jun SY, Nojiri H, Yamane H, Shoun H, Omori T, Wakagi T, Protein Sci. 2002 Sep;11(9):2184-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12192074 12192074]
[[Category: 2-hydroxymuconate-semialdehyde hydrolase]]
[[Category: 2-hydroxymuconate-semialdehyde hydrolase]]
[[Category: Pseudomonas fluorescens]]
[[Category: Pseudomonas fluorescens]]
Line 36: Line 44:
[[Category: Polychlorinated biphenyl degradation]]
[[Category: Polychlorinated biphenyl degradation]]
[[Category: Substrate specificity]]
[[Category: Substrate specificity]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:27:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:57:25 2008''

Revision as of 15:57, 28 July 2008

Image:2d0d.png

Template:STRUCTURE 2d0d

Crystal Structure of a Meta-cleavage Product Hydrolase (CumD) A129V Mutant

Template:ABSTRACT PUBMED 16844437

About this Structure

2D0D is a Single protein structure of sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA.

Reference

Improving the catalytic efficiency of a meta-cleavage product hydrolase (CumD) from Pseudomonas fluorescens IP01., Jun SY, Fushinobu S, Nojiri H, Omori T, Shoun H, Wakagi T, Biochim Biophys Acta. 2006 Jul;1764(7):1159-66. Epub 2006 Jun 7. PMID:16844437

A series of crystal structures of a meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) complexed with various cleavage products., Fushinobu S, Jun SY, Hidaka M, Nojiri H, Yamane H, Shoun H, Omori T, Wakagi T, Biosci Biotechnol Biochem. 2005 Mar;69(3):491-8. PMID:15784976

Crystal structures of a meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) complexed with cleavage products., Fushinobu S, Saku T, Hidaka M, Jun SY, Nojiri H, Yamane H, Shoun H, Omori T, Wakagi T, Protein Sci. 2002 Sep;11(9):2184-95. PMID:12192074

Page seeded by OCA on Mon Jul 28 18:57:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2d0d"
Personal tools