1sat: Difference between revisions

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[[Image:1sat.jpg|left|200px]]<br /><applet load="1sat" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1sat.jpg|left|200px]]<br /><applet load="1sat" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1sat, resolution 1.75Å" />

'''CRYSTAL STRUCTURE OF THE 50 KDA METALLO PROTEASE FROM S. MARCESCENS'''<br />

==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 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.

==About this Structure==

1SAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens] with ZN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1SAT OCA].

1SAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SAT OCA].

==Reference==

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[[Category: parallel beta roll]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 02:14:~~05 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:59:36 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1sat.jpg|left|200px]]<br /><applet load="1sat" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1sat.jpg|left|200px]]<br /><applet load="1sat" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1sat, resolution 1.75&Aring;" />
 '''CRYSTAL STRUCTURE OF THE 50 KDA METALLO PROTEASE FROM S. MARCESCENS'''<br />
 ==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 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.
 ==About this Structure==
-SAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens] with ZN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SAT OCA].
+SAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SAT OCA].
 ==Reference==
@@ Line 19: / Line 19: @@
 [[Category: parallel beta roll]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:14:05 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:59:36 2008''