2e52: Difference between revisions

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<StructureSection load='2e52' size='340' side='right'caption='[[2e52]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2e52' size='340' side='right'caption='[[2e52]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2e52]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Haein Haein]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E52 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2e52]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae_Rd_KW20 Haemophilus influenzae Rd KW20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E52 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hindIIIR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=71421 HAEIN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4] </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=2e52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e52 OCA], [https://pdbe.org/2e52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e52 RCSB], [https://www.ebi.ac.uk/pdbsum/2e52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e52 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=2e52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e52 OCA], [https://pdbe.org/2e52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e52 RCSB], [https://www.ebi.ac.uk/pdbsum/2e52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e52 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/T2D3_HAEIN T2D3_HAEIN]] Recognizes the double-stranded sequence AAGCTT and cleaves after A-1.  
[https://www.uniprot.org/uniprot/T2D3_HAEIN T2D3_HAEIN] Recognizes the double-stranded sequence AAGCTT and cleaves after A-1.
== 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=2e52 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=2e52 ConSurf].
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== Publication Abstract from PubMed ==
The three-dimensional crystal structures of HindIII bound to its cognate DNA with and without divalent cations were solved at 2.17 and 2.00 A resolution, respectively. HindIII forms a dimer. The structures showed that HindIII belongs to the EcoRI-like (alpha-class) subfamily of type II restriction endonucleases. The cognate DNA-complex structures revealed the specific DNA-recognition mechanism of HindIII by which it recognizes the palindromic sequence A/AGCTT. In the Mg(2+) ion-soaked structure the DNA was cleaved and two ions were bound at each active site, corresponding to the two-metal-ion mechanism.
Structures of restriction endonuclease HindIII in complex with its cognate DNA and divalent cations.,Watanabe N, Takasaki Y, Sato C, Ando S, Tanaka I Acta Crystallogr D Biol Crystallogr. 2009 Dec;65(Pt 12):1326-33. doi:, 10.1107/S0907444909041134. Epub 2009 Nov 17. PMID:19966419<ref>PMID:19966419</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2e52" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Haein]]
[[Category: Haemophilus influenzae Rd KW20]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Type II site-specific deoxyribonuclease]]
[[Category: Sato C]]
[[Category: Sato, C]]
[[Category: Tanaka I]]
[[Category: Tanaka, I]]
[[Category: Watanabe N]]
[[Category: Watanabe, N]]
[[Category: Hydrolase-dna complex]]

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