3a52: Difference between revisions

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<StructureSection load='3a52' size='340' side='right'caption='[[3a52]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3a52' size='340' side='right'caption='[[3a52]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3a52]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_sp._ap1 Shewanella sp. ap1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A52 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3a52]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_sp._AP1 Shewanella sp. AP1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A52 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.2&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">scap ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=177958 Shewanella sp. AP1])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3a52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a52 OCA], [https://pdbe.org/3a52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a52 RCSB], [https://www.ebi.ac.uk/pdbsum/3a52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a52 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=3a52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a52 OCA], [https://pdbe.org/3a52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a52 RCSB], [https://www.ebi.ac.uk/pdbsum/3a52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a52 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8RQU7_9GAMM Q8RQU7_9GAMM]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3a52 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3a52 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of a cold-active alkaline phosphatase from a psychrophile, Shewanella sp. (SCAP), was solved at 2.2 A. A refined model showed a homodimer with six metal-ligand sites. The arrangement of the catalytic residues resembled those of alkaline phosphatases (APs), suggesting that the reaction mechanism of SCAP was fundamentally identical to those of other APs. SCAP had two distinct structural features: (i) a loop with Arg122 that bound to the phosphate moiety of the substrate suffered no constraints from the linkage to other secondary structures, and (ii) Mg3-ligand His109 was considered to undergo repulsive effect with neighboring Trp228. The local flexibility led by these features might be an important factor in the high catalytic efficiency of SCAP at low temperatures.
Crystal structure of cold-active alkaline phosphatase from the psychrophile Shewanella sp.,Tsuruta H, Mikami B, Higashi T, Aizono Y Biosci Biotechnol Biochem. 2010 Jan;74(1):69-74. Epub 2010 Jan 7. PMID:20057143<ref>PMID:20057143</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3a52" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Alkaline phosphatase 3D structures|Alkaline phosphatase 3D structures]]
*[[Alkaline phosphatase 3D structures|Alkaline phosphatase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Shewanella sp. ap1]]
[[Category: Shewanella sp. AP1]]
[[Category: Aizono, Y]]
[[Category: Aizono Y]]
[[Category: Higashi, T]]
[[Category: Higashi T]]
[[Category: Mikami, B]]
[[Category: Mikami B]]
[[Category: Tsuruta, H]]
[[Category: Tsuruta H]]
[[Category: Hydrolase]]
[[Category: Phosphatase]]

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