View source for 8byw


==Rut B structure==
<StructureSection load='8byw' size='340' side='right'caption='[[8byw]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8byw]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BYW 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]] 1.59&#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=8byw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8byw OCA], [https://pdbe.org/8byw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8byw RCSB], [https://www.ebi.ac.uk/pdbsum/8byw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8byw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RUTB_ECOD1 RUTB_ECOD1] Hydrolyzes ureidoacrylate to form aminoacrylate and carbamate. The carbamate hydrolyzes spontaneously, thereby releasing one of the nitrogen atoms of the pyrimidine ring as ammonia and one of its carbon atoms as CO2.[HAMAP-Rule:MF_00830]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We present a detailed structure-function analysis of the ureidoacrylate amidohydrolase RutB from Eschericha coli, which is an essential enzyme of the Rut pathway for pyrimidine utilization. Crystals of selenomethionine-labeled RutB were produced, which allowed us to determine the first structure of the enzyme at a resolution of 1.9 A and to identify it as a new member of the isochorismatase-like hydrolase family. RutB was co-crystallized with the substrate analogue ureidopropionate, revealing the mode of substrate binding. Mutation of residues constituting the catalytic triad (D24A, D24N, K133A, C166A, C166S, C166T, C166Y) resulted in complete inactivation of RutB, whereas mutation of other residues close to the active site (Y29F, Y35F, N72A, W74A, W74F, E80A, E80D, S92A, S92T, S92Y, Q105A, Y136A, Y136F) leads to distinct changes of the turnover number (k(cat)) and/or the Michaelis constant (K(M)). The results of our structural and mutational studies allowed us to assign specific functions to individual residues and to formulate a plausible reaction mechanism for RutB.

Structural and Functional Characterization of the Ureidoacrylate Amidohydrolase RutB from Escherichia coli.,Busch MR, Rajendran C, Sterner R Biochemistry. 2023 Jan 4. doi: 10.1021/acs.biochem.2c00640. PMID:36599150<ref>PMID:36599150</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8byw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Busch M]]
[[Category: Rajendran C]]
[[Category: Sterner R]]