2v5j: Difference between revisions

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[[Image:2v5j.~~jpg~~|left|200px]]

[[Image:2v5j.png|left|200px]]

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~~'''~~APO CLASS II ALDOLASE HPCH~~'''~~

===APO CLASS II ALDOLASE HPCH===

~~==Overview==~~

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Microorganisms are adept at degrading chemically resistant aromatic compounds. One of the longest and most well characterized aromatic catabolic pathways is the 4-hydroxyphenylacetic acid degradation pathway of Escherichia coli. The ~~final step involves the conversion of 4-hydroxy-2-oxo-heptane-1,7-dioate into pyruvate and succinic semialdehyde. This reaction is catalyzed by 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (HpcH)~~, ~~a member of the divalent metal ion dependent class II aldolase enzymes that have great biosynthetic potential. We have solved the crystal structure of HpcH in the apo form~~, ~~and with magnesium and~~ the ~~substrate analogue oxamate bound,~~ to 1.~~6 A and 2~~.~~0 A~~, ~~respectively~~. ~~Comparison with similar structures of the homologous 2~~-~~dehydro~~-~~3-deoxygalactarate aldolase, coupled with site-directed mutagenesis data, implicate histidine 45 and arginine 70 as key catalytic residues.~~

The line below this paragraph, {{ABSTRACT_PUBMED_17881002}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17881002 is the PubMed ID number.

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==About this Structure==

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[[Category: Homoprotocatechuate]]

[[Category: Lyase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun ~~May 4 18~~:12:21 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:23:22 2008''

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-[[Image:2v5j.jpg|left|200px]]
+{{Seed}}
+[[Image:2v5j.png|left|200px]]
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 {{STRUCTURE_2v5j|  PDB=2v5j  |  SCENE=  }}
-'''APO CLASS II ALDOLASE HPCH'''
+===APO CLASS II ALDOLASE HPCH===
-==Overview==
+<!--
-Microorganisms are adept at degrading chemically resistant aromatic compounds. One of the longest and most well characterized aromatic catabolic pathways is the 4-hydroxyphenylacetic acid degradation pathway of Escherichia coli. The final step involves the conversion of 4-hydroxy-2-oxo-heptane-1,7-dioate into pyruvate and succinic semialdehyde. This reaction is catalyzed by 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (HpcH), a member of the divalent metal ion dependent class II aldolase enzymes that have great biosynthetic potential. We have solved the crystal structure of HpcH in the apo form, and with magnesium and the substrate analogue oxamate bound, to 1.6 A and 2.0 A, respectively. Comparison with similar structures of the homologous 2-dehydro-3-deoxygalactarate aldolase, coupled with site-directed mutagenesis data, implicate histidine 45 and arginine 70 as key catalytic residues.
+The line below this paragraph, {{ABSTRACT_PUBMED_17881002}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17881002 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17881002}}
 ==About this Structure==
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 [[Category: Homoprotocatechuate]]
 [[Category: Lyase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 18:12:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:23:22 2008''