1dli

<table><tr><td colspan='2'>[[1dli]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_scarlatinae"_klein_1884 "micrococcus scarlatinae" klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DLI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DLI FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDX:URIDINE-5-DIPHOSPHATE-XYLOPYRANOSE'>UDX</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/UDP-glucose_6-dehydrogenase UDP-glucose 6-dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.22 1.1.1.22] </span></td></tr>

[[https://www.uniprot.org/uniprot/UDG_STRPY UDG_STRPY]] Catalyzes the formation of UDP-glucuronic acid which is required for capsular hyaluronic acid synthesis.

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== Publication Abstract from PubMed ==

Bacterial UDP-glucose dehydrogenase (UDPGlcDH) is essential for formation of the antiphagocytic capsule that protects many virulent bacteria such as Streptococcus pyogenes andStreptococcus pneumoniae type 3 from the host's immune system. We have determined the X-ray structures of both native and Cys260Ser UDPGlcDH from S. pyogenes (74% similarity to S. pneumoniae) in ternary complexes with UDP-xylose/NAD(+) and UDP-glucuronic acid/NAD(H), respectively. The 402 residue homodimeric UDPGlcDH is composed of an N-terminal NAD(+) dinucleotide binding domain and a C-terminal UDP-sugar binding domain connected by a long (48 A) central alpha-helix. The first 290 residues of UDPGlcDH share structural homology with 6-phosphogluconate dehydrogenase, including conservation of an active site lysine and asparagine that are implicated in the enzyme mechanism. Also proposed to participate in the catalytic mechanism are a threonine and a glutamate that hydrogen bond to a conserved active site water molecule suitably positioned for general acid/base catalysis.

The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation.,Campbell RE, Mosimann SC, van De Rijn I, Tanner ME, Strynadka NC Biochemistry. 2000 Jun 13;39(23):7012-23. PMID:10841783<ref>PMID:10841783</ref>

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

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== References ==

<references/>

[[Category: Micrococcus scarlatinae klein 1884]]

[[Category: UDP-glucose 6-dehydrogenase]]

[[Category: Campbell, R E]]

[[Category: Mosimann, S C]]

[[Category: Rijn, I van de]]

[[Category: Strynadka, N C.J]]

[[Category: Tanner, M E]]

[[Category: Crystallographic dimer]]

[[Category: Ternary complex]]