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| - | {{Large structure}}
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| | ==Crystal Structure of the K. lactis Urea Amidolyase== | | ==Crystal Structure of the K. lactis Urea Amidolyase== |
| - | <StructureSection load='5i8i' size='340' side='right' caption='[[5i8i]], [[Resolution|resolution]] 6.50Å' scene=''> | + | <StructureSection load='5i8i' size='340' side='right'caption='[[5i8i]], [[Resolution|resolution]] 6.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5i8i]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_sphaerica Candida sphaerica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I8I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I8I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5i8i]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis_NRRL_Y-1140 Kluyveromyces lactis NRRL Y-1140]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I8I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I8I FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3va7|3va7]], [[4iss|4iss]]</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]] 6.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KLLA0_E08119g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284590 Candida sphaerica])</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=5i8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i8i OCA], [https://pdbe.org/5i8i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i8i RCSB], [https://www.ebi.ac.uk/pdbsum/5i8i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i8i 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=5i8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i8i OCA], [http://pdbe.org/5i8i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i8i RCSB], [http://www.ebi.ac.uk/pdbsum/5i8i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i8i ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | {{Large structure}}
| + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6CP22_KLULA Q6CP22_KLULA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Candida sphaerica]] | + | [[Category: Kluyveromyces lactis NRRL Y-1140]] |
| - | [[Category: Xiang, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Zhao, J]] | + | [[Category: Xiang S]] |
| - | [[Category: Biotin-dependent carboxylase]] | + | [[Category: Zhao J]] |
| - | [[Category: Hydrolase]]
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| - | [[Category: Hyrolase]]
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| Structural highlights
Function
Q6CP22_KLULA
Publication Abstract from PubMed
Urea is the degradation product of a wide range of nitrogen containing bio-molecules. Urea amidolyase (UA) catalyzes the conversion of urea to ammonium, the essential first step in utilizing urea as a nitrogen source. It is widely distributed in fungi, bacteria and other microorganisms, and plays an important role in nitrogen recycling in the biosphere. UA is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains, which catalyze sequential reactions. In some organisms UC and AH are encoded by separated genes. We present here structure of the Kluyveromyces lactis UA (KlUA). The structure revealed that KlUA forms a compact homo-dimer with a molecular weight of 400 kDa. Structure inspired biochemical experiments revealed the mechanism of its reaction intermediate translocation, and that the KlUA holo-enzyme formation is essential for its optimal activity. Interestingly, previous studies and ours suggest that UC and AH encoded by separated genes probably do not form a KlUA-like complex, consequently they might not catalyze the urea to ammonium conversion as efficiently.
Structure and Function of Urea Amidolyase.,Zhao J, Zhu L, Fan C, Wu Y, Xiang S Biosci Rep. 2017 Dec 20. pii: BSR20171617. doi: 10.1042/BSR20171617. PMID:29263142[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhao J, Zhu L, Fan C, Wu Y, Xiang S. Structure and Function of Urea Amidolyase. Biosci Rep. 2017 Dec 20. pii: BSR20171617. doi: 10.1042/BSR20171617. PMID:29263142 doi:http://dx.doi.org/10.1042/BSR20171617
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