1wni: Difference between revisions
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New page: left|200px<br /><applet load="1wni" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wni, resolution 2.2Å" /> '''Crystal Structure of ... |
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[[Image:1wni.gif|left|200px]]<br /><applet load="1wni" size=" | [[Image:1wni.gif|left|200px]]<br /><applet load="1wni" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1wni, resolution 2.2Å" /> | caption="1wni, resolution 2.2Å" /> | ||
'''Crystal Structure of H2-Proteinase'''<br /> | '''Crystal Structure of H2-Proteinase'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of the zinc-protease, H2-proteinase, isolated from | The crystal structure of the zinc-protease, H2-proteinase, isolated from the venom of Trimeresurus flavoviridis has been determined. The crystallographic R factor is 0.176 for 10,635 reflections with Fobs > 2sigma(Fobs) in the 8.0 to 2.2 Angstrom resolution range. The enzyme has two domains with a cleft in which a catalytic zinc atom is located. The N-terminal domain is composed of four helices around a central five-stranded beta-sheet. The irregularly folded C-terminal domain contains one helix and two disulfide bridges. These two domains are linked by a disulfide bridge. In the zinc environment, the catalytic zinc atom forms a distorted tetrahedral coordination with three histidines and one catalytic water molecule, and the methionine-containing turn is structurally conserved. These are distinctive features of the metzincins, one of the zinc metalloprotease superfamilies. The entire structure shows good agreement with that of two Crotalus snake venom proteases, adamalysin II and atrolysin C. The H2-proteinase, however, contains no structural calcium ions, and differences of disulfide configurations and the coordination of the catalytic water molecule exist as compared with the other two proteases. | ||
==About this Structure== | ==About this Structure== | ||
1WNI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trimeresurus_flavoviridis Trimeresurus flavoviridis] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trimerelysin_II Trimerelysin II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.53 3.4.24.53] Full crystallographic information is available from [http:// | 1WNI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trimeresurus_flavoviridis Trimeresurus flavoviridis] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trimerelysin_II Trimerelysin II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.53 3.4.24.53] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WNI OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of H2-proteinase from the venom of Trimeresurus flavoviridis., Kumasaka T, Yamamoto M, Moriyama H, Tanaka N, Sato M, Katsube Y, Yamakawa Y, Omori-Satoh T, Iwanaga S, Ueki T, J Biochem | Crystal structure of H2-proteinase from the venom of Trimeresurus flavoviridis., Kumasaka T, Yamamoto M, Moriyama H, Tanaka N, Sato M, Katsube Y, Yamakawa Y, Omori-Satoh T, Iwanaga S, Ueki T, J Biochem. 1996 Jan;119(1):49-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8907175 8907175] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Trimerelysin II]] | [[Category: Trimerelysin II]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:15 2008'' | ||
