View source for 3ocw


==Structure of Recombinant Haemophilus influenzae e(P4) Acid Phosphatase mutant D66N complexed with 3'-AMP==
<StructureSection load='3ocw' size='340' side='right'caption='[[3ocw]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ocw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OCW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OCW 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]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3AM:[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-4-HYDROXY-2-(HYDROXYMETHYL)OXOLAN-3-YL]+DIHYDROGEN+PHOSPHATE'>3AM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3ocw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ocw OCA], [https://pdbe.org/3ocw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ocw RCSB], [https://www.ebi.ac.uk/pdbsum/3ocw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ocw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HEL_HAEIN HEL_HAEIN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The e (P4) phosphatase from Haemophilus influenzae functions in a vestigial NAD(+) utilization pathway by dephosphorylating nicotinamide mononucleotide to nicotinamide riboside. P4 is also the prototype of class C acid phosphatases (CCAPs), which are nonspecific 5',3'-nucleotidases localized to the bacterial outer membrane. To understand substrate recognition by P4 and other class C phosphatases, we have determined the crystal structures of a substrate-trapping mutant P4 enzyme complexed with nicotinamide mononucleotide, 5'-AMP, 3'-AMP, and 2'-AMP. The structures reveal an anchor-shaped substrate-binding cavity comprising a conserved hydrophobic box that clamps the nucleotide base, a buried phosphoryl binding site, and three solvent-filled pockets that contact the ribose and the hydrogen-bonding edge of the base. The span between the hydrophobic box and the phosphoryl site is optimal for recognizing nucleoside monophosphates, explaining the general preference for this class of substrate. The base makes no hydrogen bonds with the enzyme, consistent with an observed lack of base specificity. Two solvent-filled pockets flanking the ribose are key to the dual recognition of 5'-nucleotides and 3'-nucleotides. These pockets minimize the enzyme's direct interactions with the ribose and provide sufficient space to accommodate 5' substrates in an anti conformation and 3' substrates in a syn conformation. Finally, the structures suggest that class B acid phosphatases and CCAPs share a common strategy for nucleotide recognition.

Recognition of nucleoside monophosphate substrates by Haemophilus influenzae class C acid phosphatase.,Singh H, Schuermann JP, Reilly TJ, Calcutt MJ, Tanner JJ J Mol Biol. 2010 Dec 10;404(4):639-49. Epub 2010 Oct 8. PMID:20934434<ref>PMID:20934434</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ocw" style="background-color:#fffaf0;"></div>

==See Also==
*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Haemophilus influenzae]]
[[Category: Large Structures]]
[[Category: Calcutt M]]
[[Category: Reilly T]]
[[Category: Schuermann J]]
[[Category: Singh H]]
[[Category: Tanner J]]