6zla

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
==Crystal Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with NAD==
==Crystal Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with NAD==
-
<StructureSection load='6zla' size='340' side='right'caption='[[6zla]]' scene=''>
+
<StructureSection load='6zla' size='340' side='right'caption='[[6zla]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZLA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZLA FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6zla]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZLA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZLA FirstGlance]. <br>
-
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6zla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zla OCA], [http://pdbe.org/6zla PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zla RCSB], [http://www.ebi.ac.uk/pdbsum/6zla PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zla ProSAT]</span></td></tr>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IG7_05634 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 ATCC 14579])</td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6zla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zla OCA], [http://pdbe.org/6zla PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zla RCSB], [http://www.ebi.ac.uk/pdbsum/6zla PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zla ProSAT]</span></td></tr>
</table>
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
UDP-glucuronic acid is converted to UDP-galacturonic acid en route to a variety of sugar-containing metabolites. This reaction is performed by a NAD(+)-dependent epimerase belonging to the short-chain dehydrogenase/reductase family. We present several high-resolution crystal structures of the UDP-glucuronic acid epimerase from Bacillus cereus The geometry of the substrate-NAD(+) interactions is finely arranged to promote hydride transfer. The exquisite complementarity between glucuronic acid and its binding site is highlighted by the observation that the unligated cavity is occupied by a cluster of ordered waters whose positions overlap the polar groups of the sugar substrate. Co-crystallization experiments led to a structure where substrate- and product-bound enzymes coexist within the same crystal. This equilibrium structure reveals the basis for a "swing &amp; flip" rotation of the pro-chiral 4-keto-hexose-uronic acid intermediate that results from glucuronic acid oxidation, placing the C4' atom in position for receiving a hydride ion on the opposite side of the sugar ring. The product-bound active site is almost identical to that of the substrate-bound structure and satisfies all hydrogen-bonding requirements of the ligand. The structure of the apo-enzyme together with kinetic isotope effect and mutagenesis experiments further outlines a few flexible loops that exist in discrete conformations, imparting structural malleability required for ligand rotation while avoiding leakage of the catalytic intermediate and/or side-reactions. These data highlight the double nature of the enzymatic mechanism: the active site features a high degree of precision in substrate recognition combined with the flexibility required for intermediate rotation.
 +
 +
Crystallographic snapshots of UDP-glucuronic acid 4-epimeraseligand binding, rotation and reduction.,Iacovino LG, Savino S, Borg AJE, Binda C, Nidetzky B, Mattevi A J Biol Chem. 2020 Jul 13. pii: RA120.014692. doi: 10.1074/jbc.RA120.014692. PMID:32661196<ref>PMID:32661196</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 6zla" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Atcc 14579]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Iacovino LG]]
+
[[Category: Iacovino, L G]]
-
[[Category: Mattevi A]]
+
[[Category: Mattevi, A]]
 +
[[Category: Epimerase]]
 +
[[Category: Nad]]
 +
[[Category: Oxidoreductase]]
 +
[[Category: Udp-sugar binding protein]]

Revision as of 10:02, 9 September 2020

Crystal Structure of UDP-Glucuronic acid 4-epimerase from Bacillus cereus in complex with NAD

PDB ID 6zla

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools