View source for 6vxc


==Crystal structure of hydroxyproline dehydratase (HypD) from Clostridioides difficile==
<StructureSection load='6vxc' size='340' side='right'caption='[[6vxc]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6vxc]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile_70-100-2010 Clostridioides difficile 70-100-2010]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VXC 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]] 2.05&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vxc OCA], [https://pdbe.org/6vxc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vxc RCSB], [https://www.ebi.ac.uk/pdbsum/6vxc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vxc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q180C6_CLOD6 Q180C6_CLOD6] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The glycyl radical enzyme (GRE) superfamily utilizes a glycyl radical cofactor to catalyze difficult chemical reactions in a variety of anaerobic microbial metabolic pathways. Recently, a GRE, trans-4-hydroxy-L-proline (Hyp) dehydratase (HypD), was discovered that catalyzes the dehydration of Hyp to (S)-Delta(1)-pyrroline-5-carboxylic acid (P5C). This enzyme is abundant in the human gut microbiome and also present in prominent bacterial pathogens. However, we lack an understanding of how HypD performs its unusual chemistry. Here, we have solved the crystal structure of HypD from the pathogen Clostridioides difficile with Hyp bound in the active site. Biochemical studies have led to the identification of key catalytic residues and have provided insight into the radical mechanism of Hyp dehydration.

Molecular basis for catabolism of the abundant metabolite trans-4-hydroxy-L-proline by a microbial glycyl radical enzyme.,Backman LR, Huang YY, Andorfer MC, Gold B, Raines RT, Balskus EP, Drennan CL Elife. 2020 Mar 17;9. pii: 51420. doi: 10.7554/eLife.51420. PMID:32180548<ref>PMID:32180548</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6vxc" style="background-color:#fffaf0;"></div>

==See Also==
*[[HypA%2C HypB%2C HypC%2C HypD%2C HypE and HypF 3D structures|HypA%2C HypB%2C HypC%2C HypD%2C HypE and HypF 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridioides difficile 70-100-2010]]
[[Category: Large Structures]]
[[Category: Backman LRF]]
[[Category: Drennan CL]]