5i8i: Difference between revisions

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'''Unreleased structure'''


The entry 5i8i is ON HOLD  until Paper Publication
==Crystal Structure of the K. lactis Urea Amidolyase==
<StructureSection load='5i8i' size='340' side='right'caption='[[5i8i]], [[Resolution|resolution]] 6.50&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 6.5&#8491;</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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6CP22_KLULA Q6CP22_KLULA]
<div style="background-color:#fffaf0;">
== 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.


Authors: Zhao, J., Xiang, S.
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<ref>PMID:29263142</ref>


Description: Crystal Structure of the K. lactis Urea Amidolyase
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Zhao, J]]
<div class="pdbe-citations 5i8i" style="background-color:#fffaf0;"></div>
[[Category: Xiang, S]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Kluyveromyces lactis NRRL Y-1140]]
[[Category: Large Structures]]
[[Category: Xiang S]]
[[Category: Zhao J]]
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