1dhn: Difference between revisions

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New page: left|200px<br /><applet load="1dhn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dhn, resolution 1.65Å" /> '''1.65 ANGSTROM RESOLU...
 
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[[Image:1dhn.gif|left|200px]]<br /><applet load="1dhn" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dhn.gif|left|200px]]<br /><applet load="1dhn" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dhn, resolution 1.65&Aring;" />
caption="1dhn, resolution 1.65&Aring;" />
'''1.65 ANGSTROM RESOLUTION STRUCTURE OF 7,8-DIHYDRONEOPTERIN ALDOLASE FROM STAPHYLOCOCCUS AUREUS'''<br />
'''1.65 ANGSTROM RESOLUTION STRUCTURE OF 7,8-DIHYDRONEOPTERIN ALDOLASE FROM STAPHYLOCOCCUS AUREUS'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1DHN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DHN OCA].  
1DHN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHN OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Arcy, A.D.]]
[[Category: Arcy, A D.]]
[[Category: Dale, G.]]
[[Category: Dale, G.]]
[[Category: Hampele, I.C.]]
[[Category: Hampele, I C.]]
[[Category: Hennig, M.]]
[[Category: Hennig, M.]]
[[Category: Oefner, C.H.]]
[[Category: Oefner, C H.]]
[[Category: Page, M.G.P.]]
[[Category: Page, M G.P.]]
[[Category: antibiotic target]]
[[Category: antibiotic target]]
[[Category: beta-barrel]]
[[Category: beta-barrel]]
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[[Category: pterine binding]]
[[Category: pterine binding]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:17:22 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:16:39 2008''