1dhn

<table><tr><td colspan='2'>[[1dhn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1DHN FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DHNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1dhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhn OCA], [http://pdbe.org/1dhn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dhn RCSB], [http://www.ebi.ac.uk/pdbsum/1dhn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dhn ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/FOLB_STAAU FOLB_STAAU]] Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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<ref>PMID:9586996</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1dhn" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Arcy, A D]]

[[Category: Dale, G]]

[[Category: Hampele, I C]]

[[Category: Hennig, M]]

[[Category: Oefner, C H]]

[[Category: Page, M G.P]]

[[Category: Pterin binding]]