1mee: Difference between revisions

Revision as of 14:54, 21 February 2008

THE COMPLEX BETWEEN THE SUBTILISIN FROM A MESOPHILIC BACTERIUM AND THE LEECH INHIBITOR EGLIN-C

OverviewOverview

The alkaline proteinase from the mesophilic bacterium Bacillus mesentericus has been crystallized in a 1:1 complex with the inhibitor eglin-C from the medical leech. The crystals have cell dimensions of a = 43.0, b = 71.9, c = 48.3 A and beta = 110.0 degrees and are in the space group P2(1). Three-dimensional data to 2.0 A have been recorded on film from a single crystal. The orientation and position of the complex in the unit cell have been established using the refined coordinates of subtilisin Carlsberg and of eglin-C as independent models. The structure of the complex has been refined by restrained least-squares minimization. The crystallographic R factor (= sigma[magnitude of Fo - magnitude of Fc[/sigma magnitude of Fo) is 15.1% including two Ca2+ ions and 312 water molecules. The structure is discussed in terms of its physicochemical properties in solution and its relation to other Bacillus subtilisins.

About this StructureAbout this Structure

1MEE is a Protein complex structure of sequences from Bacillus pumilus and Hirudo medicinalis with as ligand. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.

ReferenceReference

Complex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-C., Dauter Z, Betzel C, Genov N, Pipon N, Wilson KS, Acta Crystallogr B. 1991 Oct 1;47 ( Pt 5):707-30. PMID:1793542

Page seeded by OCA on Thu Feb 21 13:54:24 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1mee.gif|left|200px]]<br /><applet load="1mee" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1mee.gif|left|200px]]<br /><applet load="1mee" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1mee, resolution 2.0&Aring;" />
 '''THE COMPLEX BETWEEN THE SUBTILISIN FROM A MESOPHILIC BACTERIUM AND THE LEECH INHIBITOR EGLIN-C'''<br />
 ==Overview==
-The alkaline proteinase from the mesophilic bacterium Bacillus, mesentericus has been crystallized in a 1:1 complex with the inhibitor, eglin-C from the medical leech. The crystals have cell dimensions of a =, 43.0, b = 71.9, c = 48.3 A and beta = 110.0 degrees and are in the space, group P2(1). Three-dimensional data to 2.0 A have been recorded on film, from a single crystal. The orientation and position of the complex in the, unit cell have been established using the refined coordinates of, subtilisin Carlsberg and of eglin-C as independent models. The structure, of the complex has been refined by restrained least-squares minimization., The crystallographic R factor (= sigma[magnitude of Fo - magnitude of, Fc[/sigma magnitude of Fo) is 15.1% including two Ca2+ ions and 312 water, molecules. The structure is discussed in terms of its physicochemical, properties in solution and its relation to other Bacillus subtilisins.
+The alkaline proteinase from the mesophilic bacterium Bacillus mesentericus has been crystallized in a 1:1 complex with the inhibitor eglin-C from the medical leech. The crystals have cell dimensions of a = 43.0, b = 71.9, c = 48.3 A and beta = 110.0 degrees and are in the space group P2(1). Three-dimensional data to 2.0 A have been recorded on film from a single crystal. The orientation and position of the complex in the unit cell have been established using the refined coordinates of subtilisin Carlsberg and of eglin-C as independent models. The structure of the complex has been refined by restrained least-squares minimization. The crystallographic R factor (= sigma[magnitude of Fo - magnitude of Fc[/sigma magnitude of Fo) is 15.1% including two Ca2+ ions and 312 water molecules. The structure is discussed in terms of its physicochemical properties in solution and its relation to other Bacillus subtilisins.
 ==About this Structure==
-MEE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_pumilus Bacillus pumilus] and [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MEE OCA].
+MEE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_pumilus Bacillus pumilus] and [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MEE OCA].
 ==Reference==
@@ Line 17: / Line 17: @@
 [[Category: Betzel, C.]]
 [[Category: Dauter, Z.]]
-[[Category: Wilson, K.S.]]
+[[Category: Wilson, K S.]]
 [[Category: CA]]
 [[Category: complex(serine proteinase-inhibitor)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:22:11 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:24 2008''