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| | ==Structure of Giardia Carbamate Kinase== | | ==Structure of Giardia Carbamate Kinase== |
| - | <StructureSection load='3kzf' size='340' side='right' caption='[[3kzf]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='3kzf' size='340' side='right'caption='[[3kzf]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3kzf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Giaic Giaic]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KZF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KZF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3kzf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Giardia_lamblia_ATCC_50803 Giardia lamblia ATCC 50803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KZF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KZF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CK, GL50803_16453 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=184922 GIAIC])</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></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbamate_kinase Carbamate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.2 2.7.2.2] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3kzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kzf OCA], [https://pdbe.org/3kzf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kzf RCSB], [https://www.ebi.ac.uk/pdbsum/3kzf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kzf ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kzf OCA], [http://pdbe.org/3kzf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kzf RCSB], [http://www.ebi.ac.uk/pdbsum/3kzf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kzf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A8BB85_GIAIC A8BB85_GIAIC] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Carbamate kinase]] | + | [[Category: Giardia lamblia ATCC 50803]] |
| - | [[Category: Giaic]] | + | [[Category: Large Structures]] |
| - | [[Category: Galkin, A]] | + | [[Category: Galkin A]] |
| - | [[Category: Herzberg, O]] | + | [[Category: Herzberg O]] |
| - | [[Category: Arginine dihydrolase pathway]]
| + | |
| - | [[Category: Drug target]]
| + | |
| - | [[Category: Giardia lamblia]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
A8BB85_GIAIC
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Carbamate kinase catalyzes the reversible conversion of carbamoyl phosphate and ADP to ATP and ammonium carbamate, which is hydrolyzed to ammonia and carbonate. The three-dimensional structure of carbamate kinase from the human parasite Giardia lamblia (glCK) has been determined at 3 A resolution. The crystals belonged to the monoclinic space group P2(1), with unit-cell parameters a = 69.77, b = 85.41, c = 102.1 A, beta = 106.8 degrees . The structure was refined to a final R factor of 0.227. The essentiality of glCK together with its absence in humans makes the enzyme an attractive candidate for anti-Giardia drug development. Steady-state kinetic rate constants have been determined. The k(cat) for ATP formation is 319 +/- 9 s(-1). The K(m) values for carbamoyl phosphate and ADP are 85 +/- 6 and 70 +/- 5 microM, respectively. The structure suggests that three invariant lysine residues (Lys131, Lys216 and Lys278) may be involved in the binding of substrates and phosphoryl transfer. The structure of glCK reveals that a glycerol molecule binds in the likely carbamoyl phosphate-binding site.
X-ray structure and characterization of carbamate kinase from the human parasite Giardia lamblia.,Galkin A, Kulakova L, Wu R, Nash TE, Dunaway-Mariano D, Herzberg O Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Apr 1;66(Pt 4):386-90., Epub 2010 Mar 26. PMID:20383005[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Galkin A, Kulakova L, Wu R, Nash TE, Dunaway-Mariano D, Herzberg O. X-ray structure and characterization of carbamate kinase from the human parasite Giardia lamblia. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Apr 1;66(Pt 4):386-90., Epub 2010 Mar 26. PMID:20383005 doi:10.1107/S1744309110004665
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