1ogh

<table><tr><td colspan='2'>[[1ogh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OGH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OGH FirstGlance]. <br>

</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=1ogh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ogh OCA], [http://pdbe.org/1ogh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ogh RCSB], [http://www.ebi.ac.uk/pdbsum/1ogh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ogh ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/DCD_METJA DCD_METJA]] Catalyzes two consecutive reactions to form dUMP using dCTP as substrate.[HAMAP-Rule:MF_00146]

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== Publication Abstract from PubMed ==

The bifunctional dCTP deaminase-dUTPase (DCD-DUT) from Methanocaldococcus jannaschii catalyzes the deamination of the cytosine moiety in dCTP and the hydrolysis of the triphosphate moiety forming dUMP, thereby preventing uracil from being incorporated into DNA. The crystal structure of DCD-DUT has been determined to 1.88-A resolution and represents the first known structure of an enzyme catalyzing dCTP deamination. The functional form of DCD-DUT is a homotrimer wherein the subunits are composed of a central distorted beta-barrel surrounded by two beta-sheets and four helices. The trimeric DCD-DUT shows structural similarity to trimeric dUTPases at the tertiary and quaternary levels. There are also additional structural elements in DCD-DUT compared with dUTPase because of a longer primary structure. Four of the five conserved sequence motifs that create the active sites in dUTPase are found in structurally equivalent positions in DCD-DUT. The last 25 C-terminal residues of the 204-residue-long DCD-DUT are not visible in the electron density map, but, analogous to dUTPases, the C terminus is probably ordered, closing the active site upon catalysis. Unlike other enzymes catalyzing the deamination of cytosine compounds, DCD-DUT is not exploiting an enzyme-bound metal ion such as zinc or iron for nucleophile generation. The active site contains two water molecules that are engaged in hydrogen bonds to the invariant residues Ser118, Arg122, Thr130, and Glu145. These water molecules are potential nucleophile candidates in the deamination reaction.

Structure of the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii and its relation to other homotrimeric dUTPases.,Johansson E, Bjornberg O, Nyman PO, Larsen S J Biol Chem. 2003 Jul 25;278(30):27916-22. Epub 2003 May 19. PMID:12756253<ref>PMID:12756253</ref>

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

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

[[Category: Atcc 43067]]

[[Category: Bjornberg, O]]

[[Category: Johansson, E]]

[[Category: Nyman, P O]]

[[Category: Bifunctional enzyme]]

[[Category: Dctp deaminase]]

[[Category: Dutpase]]

[[Category: Nucleotide metabolism]]