7d2f

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (16:24, 29 November 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='7d2f' size='340' side='right'caption='[[7d2f]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='7d2f' size='340' side='right'caption='[[7d2f]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[7d2f]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D2F FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[7d2f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_str._Philadelphia_1 Legionella pneumophila subsp. pneumophila str. Philadelphia 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D2F FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] </span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</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=7d2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d2f OCA], [https://pdbe.org/7d2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d2f RCSB], [https://www.ebi.ac.uk/pdbsum/7d2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d2f ProSAT]</span></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=7d2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d2f OCA], [https://pdbe.org/7d2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d2f RCSB], [https://www.ebi.ac.uk/pdbsum/7d2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d2f ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/Q5ZWG6_LEGPH Q5ZWG6_LEGPH]
-
MapA is a histidine acid phosphatase (HAP) from Legionella pneumophila that catalyzes the hydroxylation of a phosphoryl group from phosphomonoesters by an active-site histidine. Several structures of HAPs, including MapA, in complex with the inhibitor tartrate have been solved and the substrate binding tunnel identified; however, the substrate recognition mechanism remains unknown. To gain insight into the mechanism of substrate recognition, the crystal structures of apo-MapA and the MapA(D281A) mutant in complex with 5'-AMP were solved at 2.2 and 2.6 A resolution, respectively. The structure of the MapA(D281A)/5'-AMP complex reveals that the 5'-AMP fits fully into the substrate binding tunnel, with the 2'-hydroxyl group of the ribose moiety stabilized by Glu201 and the adenine moiety sandwiched between His205 and Phe237. This is the second structure of a HAP/AMP complex solved with 5'-AMP binding in a unique manner in the active site. The structure presents a new substrate recognition mechanism of HAPs.
+
-
Structural insights into a new substrate binding mode of a histidine acid phosphatase from Legionella pneumophila.,Guo Y, Zhou D, Zhang H, Zhang NN, Qi X, Chen X, Chen Q, Li J, Ge H, Teng YB Biochem Biophys Res Commun. 2021 Feb 12;540:90-94. doi:, 10.1016/j.bbrc.2020.12.070. Epub 2021 Jan 12. PMID:33450485<ref>PMID:33450485</ref>
+
==See Also==
-
 
+
*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 7d2f" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Acid phosphatase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Guo, Y]]
+
[[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]]
-
[[Category: Teng, Y]]
+
[[Category: Guo Y]]
-
[[Category: 5'-amp]]
+
[[Category: Teng Y]]
-
[[Category: Complex]]
+
-
[[Category: Hydrolase]]
+

Current revision

Lp major histidine acid phosphatase mutant D281A/5'-AMP

PDB ID 7d2f

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7d2f"
Personal tools