1sat: Difference between revisions

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[[Image:1sat.~~jpg~~|left|200px]]

[[Image:1sat.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF THE 50 KDA METALLO PROTEASE FROM S. MARCESCENS~~'''~~

===CRYSTAL STRUCTURE OF THE 50 KDA METALLO PROTEASE FROM S. MARCESCENS===

~~==Overview==~~

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The ~~crystal structure of~~ the ~~50 kDa metalloprotease from~~ the ~~Gram-negative bacterium Serratia marcescens has been solved and refined to a crystallographic R-factor of 0.192~~ at ~~1.80 A resolution. The structure is very similar to that of alkaline protease from Pseudomonas aeruginosa, in particular the calcium binding "parallel beta roll" motif is completely conserved~~. ~~The N-terminal proteolytic domain shows the typical "metzincin" fold~~. ~~The active sites of the two enzymes are slightly different~~, ~~Tyr216~~ is ~~a Zn ligand in~~ the ~~Serratia metallo protease~~. ~~The loops 70~~-~~77 and 122~~-~~132, which encompass the active site cleft, differ due to insertions and deletions so that the Serratia metallo protease seems to have a more open site than the alkaline protease.~~

The line below this paragraph, {{ABSTRACT_PUBMED_8089845}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8089845 is the PubMed ID number.

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==About this Structure==

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[[Category: Parallel beta helix]]

[[Category: Parallel beta roll]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 08~~:29:31 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:58:23 2008''

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-[[Image:1sat.jpg|left|200px]]
+{{Seed}}
+[[Image:1sat.png|left|200px]]
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 {{STRUCTURE_1sat|  PDB=1sat  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE 50 KDA METALLO PROTEASE FROM S. MARCESCENS'''
+===CRYSTAL STRUCTURE OF THE 50 KDA METALLO PROTEASE FROM S. MARCESCENS===
-==Overview==
+<!--
-The crystal structure of the 50 kDa metalloprotease from the Gram-negative bacterium Serratia marcescens has been solved and refined to a crystallographic R-factor of 0.192 at 1.80 A resolution. The structure is very similar to that of alkaline protease from Pseudomonas aeruginosa, in particular the calcium binding "parallel beta roll" motif is completely conserved. The N-terminal proteolytic domain shows the typical "metzincin" fold. The active sites of the two enzymes are slightly different, Tyr216 is a Zn ligand in the Serratia metallo protease. The loops 70-77 and 122-132, which encompass the active site cleft, differ due to insertions and deletions so that the Serratia metallo protease seems to have a more open site than the alkaline protease.
+The line below this paragraph, {{ABSTRACT_PUBMED_8089845}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8089845 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8089845}}
 ==About this Structure==
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 [[Category: Parallel beta helix]]
 [[Category: Parallel beta roll]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:29:31 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:58:23 2008''