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1dlj

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[[Image:1dlj.gif|left|200px]]
 
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{{Structure
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==THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION==
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|PDB= 1dlj |SIZE=350|CAPTION= <scene name='initialview01'>1dlj</scene>, resolution 1.80&Aring;
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<StructureSection load='1dlj' size='340' side='right'caption='[[1dlj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UGA:URIDINE-5&#39;-DIPHOSPHATE-GLUCURONIC+ACID'>UGA</scene>
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<table><tr><td colspan='2'>[[1dlj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DLJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DLJ FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-glucose_6-dehydrogenase UDP-glucose 6-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.22 1.1.1.22] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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|GENE=
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<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=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UGA:URIDINE-5-DIPHOSPHATE-GLUCURONIC+ACID'>UGA</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dlj OCA], [https://pdbe.org/1dlj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dlj RCSB], [https://www.ebi.ac.uk/pdbsum/1dlj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dlj ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1dli|1DLI]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dlj OCA], [http://www.ebi.ac.uk/pdbsum/1dlj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dlj RCSB]</span>
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== Function ==
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}}
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[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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== Evolutionary Conservation ==
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'''THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dl/1dlj_consurf.spt"</scriptWhenChecked>
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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.
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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1DLJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DLJ OCA].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dlj ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10841783 10841783]
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</StructureSection>
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[[Category: Single protein]]
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[[Category: Large Structures]]
[[Category: Streptococcus pyogenes]]
[[Category: Streptococcus pyogenes]]
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[[Category: UDP-glucose 6-dehydrogenase]]
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[[Category: Campbell RE]]
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[[Category: Campbell, R E.]]
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[[Category: Mosimann SC]]
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[[Category: Mosimann, S C.]]
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[[Category: Strynadka NCJ]]
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[[Category: Rijn, I van de.]]
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[[Category: Tanner ME]]
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[[Category: Strynadka, N C.J.]]
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[[Category: Van de Rijn I]]
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[[Category: Tanner, M E.]]
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[[Category: crystallographic dimer]]
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[[Category: rossmann fold]]
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[[Category: ternary complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:43:51 2008''
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Current revision

THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION

PDB ID 1dlj

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