1dhn

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{{STRUCTURE_1dhn| PDB=1dhn | SCENE= }}
{{STRUCTURE_1dhn| PDB=1dhn | SCENE= }}
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'''1.65 ANGSTROM RESOLUTION STRUCTURE OF 7,8-DIHYDRONEOPTERIN ALDOLASE FROM STAPHYLOCOCCUS AUREUS'''
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===1.65 ANGSTROM RESOLUTION STRUCTURE OF 7,8-DIHYDRONEOPTERIN ALDOLASE FROM STAPHYLOCOCCUS AUREUS===
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==Overview==
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Dihydroneopterin aldolase catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin during the de novo synthesis of folic acid from guanosine triphosphate. The gene encoding the dihydroneopterin aldolase from S. aureus has been cloned, sequenced and expressed in Escherichia coli. The protein has been purified for biochemical characterization and its X-ray structure determined at 1.65 A resolution. The protein forms an octamer of 110,000 Mr molecular weight. Four molecules assemble into a ring, and two rings come together to give a cylinder with a hole of at least 13 A diameter. The structure of the binary complex with the product 6-hydroxymethyl-7,8-dihydropterin has defined the location of the active site. The structural information and results of site directed mutagenesis allow an enzyme reaction mechanism to be proposed.
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{{ABSTRACT_PUBMED_9586996}}
==About this Structure==
==About this Structure==
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[[Category: Folate biosynthesis]]
[[Category: Folate biosynthesis]]
[[Category: Pterine binding]]
[[Category: Pterine binding]]
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Revision as of 20:04, 30 June 2008

Image:1dhn.png

Template:STRUCTURE 1dhn

1.65 ANGSTROM RESOLUTION STRUCTURE OF 7,8-DIHYDRONEOPTERIN ALDOLASE FROM STAPHYLOCOCCUS AUREUS

Template:ABSTRACT PUBMED 9586996

About this Structure

1DHN is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from Staphylococcus aureus., Hennig M, D'Arcy A, Hampele IC, Page MG, Oefner C, Dale GE, Nat Struct Biol. 1998 May;5(5):357-62. PMID:9586996

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