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4dzt
From Proteopedia
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| - | [[ | + | ==Aqualysin I: the crystal structure of a serine protease from an extreme thermophile, Thermus aquaticus YT-1== |
| + | <StructureSection load='4dzt' size='340' side='right' caption='[[4dzt]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4dzt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DZT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DZT FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PMS:PHENYLMETHANESULFONIC+ACID'>PMS</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2prk|2prk]], [[1sup|1sup]], [[2gko|2gko]], [[1svn|1svn]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aqualysin_1 Aqualysin 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.111 3.4.21.111] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4dzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dzt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dzt RCSB], [http://www.ebi.ac.uk/pdbsum/4dzt PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Aqualysin I, a thermostable protease found in the culture medium of Thermus aquaticus YT-1, has been purified to homogeneity using a combination of ion-exchange and affinity chromatography. It is a polypeptide with a molecular weight of 28 350 [Kwon, Terada, Matsuzawa & Ohta (1988). Eur. J. Biochem. 173, 491-497] and is most active at 343-353 K and pH about 10.0 [Matsuzawa, Tokugawa, Hamaoki, Mizoguchi, Taguchi, Terada, Kwon & Ohta (1988). Eur. J. Biochem. 171, 441-447]. Crystals of the enzyme are monoclinic, space group P2(1), with cell dimensions a = 40.80 (5), b = 64.39 (6), c = 45.51 (6) A and beta = 109.1 (1) degrees. The asymmetric unit consists of a single molecule (V(m) = 1.99 A(3)Da(-1)). The crystals are stable to X-radiation and scatter to at least 2.8 A resolution. | ||
| - | + | Purification, crystallization and preliminary X-ray investigation of aqualysin I, a heat-stable serine protease.,Green PR, Oliver JD, Strickland LC, Toerner DR, Matsuzawa H, Ohta T Acta Crystallogr D Biol Crystallogr. 1993 May 1;49(Pt 3):349-52. PMID:15299524<ref>PMID:15299524</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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| - | == | + | |
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[[Category: Aqualysin 1]] | [[Category: Aqualysin 1]] | ||
[[Category: Thermus aquaticus]] | [[Category: Thermus aquaticus]] | ||
Revision as of 07:22, 5 June 2014
Aqualysin I: the crystal structure of a serine protease from an extreme thermophile, Thermus aquaticus YT-1
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