2dch

<table><tr><td colspan='2'>[[2dch]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoproteus Thermoproteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DCH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DCH FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dch OCA], [http://pdbe.org/2dch PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dch RCSB], [http://www.ebi.ac.uk/pdbsum/2dch PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dch ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

A novel LAGLIDADG-type homing endonuclease (HEase), I-Tsp061I, from the hyperthermophilic archaeon Thermoproteus sp. IC-061 16 S rRNA gene (rDNA) intron was characterized with respect to its structure, catalytic properties and thermostability. It was found that I-Tsp061I is a HEase isoschizomer of the previously described I-PogI and exhibits the highest thermostability among the known LAGLIDADG-type HEases. Determination of the crystal structure of I-Tsp061I at 2.1 A resolution using the multiple isomorphous replacement and anomalous scattering method revealed that the overall fold is similar to that of other known LAGLIDADG-type HEases, despite little sequence similarity between I-Tsp061I and those HEases. However, I-Tsp061I contains important cross-domain polar networks, unlike its mesophilic counterparts. Notably, the polar network Tyr6-Asp104-His180-107O-HOH12-104O-Asn177 exists across the two packed alpha-helices containing both the LAGLIDADG catalytic motif and the GxxxG hydrophobic helix bundle motif. Another important structural feature is the salt-bridge network Asp29-Arg31-Glu182 across N and C-terminal domain interface, which appears to contribute to the stability of the domain/domain packing. On the basis of these structural analyses and extensive mutational studies, we conclude that such cross-domain polar networks play key roles in stabilizing the catalytic center and domain packing, and underlie the hyperthermostability of I-Tsp061I.

Structure of a hyperthermophilic archaeal homing endonuclease, I-Tsp061I: contribution of cross-domain polar networks to thermostability.,Nakayama H, Shimamura T, Imagawa T, Shirai N, Itoh T, Sako Y, Miyano M, Sakuraba H, Ohshima T, Nomura N, Tsuge H J Mol Biol. 2007 Jan 12;365(2):362-78. Epub 2006 Sep 29. PMID:17069851<ref>PMID:17069851</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Miyano, M]]

[[Category: Nakayama, H]]

[[Category: Nomura, N]]

[[Category: Sako, Y]]

[[Category: Shimamura, T]]

[[Category: Tsuge, H]]

[[Category: Hydrolase]]