1spb: Difference between revisions

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

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

caption="1spb, resolution 2.0Å" />

'''SUBTILISIN BPN' PROSEGMENT (77 RESIDUES) COMPLEXED WITH A MUTANT SUBTILISIN BPN' (266 RESIDUES). CRYSTAL PH 4.6. CRYSTALLIZATION TEMPERATURE 20 C DIFFRACTION TEMPERATURE-160 C'''<br />

==Overview==

BACKGROUND: The folding of the bacterial protease subtilisin BPN' (SBT) is, dependent on its 77-residue prosegment, which is then autocatalytically, removed to give the mature enzyme. Mature subtilisin represents a class of, proteins that lacks an efficient folding pathway. Refolding of mature SBT, is extremely slow unless catalyzed by the independently expressed, prosegment, leading to a bimolecular complex. RESULTS: We report the, crystal structure at 2.0 A resolution of the prosegment-SBT complex and, consider its implications for prosubtilisin BPN' maturation and folding, catalysis. The prosegment forms a compact domain that binds SBT through an, extensive interface involving the enzyme's two parallel surface helices, (residues 104-116 and 133-144), supplying negatively charged caps to the N, termini of these helices. The prosegment C terminus binds in the enzyme, active site in a product-like manner, with Tyr77 in the P1 binding pocket., CONCLUSIONS: The structure of the complex supports a unimolecular, mechanism for prosubtilisin cleavage, involving a 25 A rearrangement of, the SBT N terminus in a late folding step. A mechanism of folding, catalysis in which the two helices and their connecting beta strand form a, prosegment-stabilized folding nucleus is proposed. While this putative, nucleus is stabilized by prosegment binding, the N-terminal and C-terminal, subdomains of SBT could fold by propagation.

BACKGROUND: The folding of the bacterial protease subtilisin BPN' (SBT) is dependent on its 77-residue prosegment, which is then autocatalytically removed to give the mature enzyme. Mature subtilisin represents a class of proteins that lacks an efficient folding pathway. Refolding of mature SBT is extremely slow unless catalyzed by the independently expressed prosegment, leading to a bimolecular complex. RESULTS: We report the crystal structure at 2.0 A resolution of the prosegment-SBT complex and consider its implications for prosubtilisin BPN' maturation and folding catalysis. The prosegment forms a compact domain that binds SBT through an extensive interface involving the enzyme's two parallel surface helices (residues 104-116 and 133-144), supplying negatively charged caps to the N termini of these helices. The prosegment C terminus binds in the enzyme active site in a product-like manner, with Tyr77 in the P1 binding pocket. CONCLUSIONS: The structure of the complex supports a unimolecular mechanism for prosubtilisin cleavage, involving a 25 A rearrangement of the SBT N terminus in a late folding step. A mechanism of folding catalysis in which the two helices and their connecting beta strand form a prosegment-stabilized folding nucleus is proposed. While this putative nucleus is stabilized by prosegment binding, the N-terminal and C-terminal subdomains of SBT could fold by propagation.

==About this Structure==

1SPB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] with NA 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=1SPB OCA].

1SPB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] with <scene name='pdbligand=NA:'>NA</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=1SPB OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Subtilisin]]

[[Category: Bryan, P.N.]]

[[Category: Bryan, P N.]]

[[Category: Gallagher, D.T.]]

[[Category: Gallagher, D T.]]

[[Category: Gilliland, G.L.]]

[[Category: Gilliland, G L.]]

[[Category: Wang, L.]]

[[Category: NA]]

Line 24:

[[Category: propeptide]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 02:32:~~37 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:03:51 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1spb.gif|left|200px]]<br /><applet load="1spb" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1spb.gif|left|200px]]<br /><applet load="1spb" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1spb, resolution 2.0&Aring;" />
 '''SUBTILISIN BPN' PROSEGMENT (77 RESIDUES) COMPLEXED WITH A MUTANT SUBTILISIN BPN' (266 RESIDUES). CRYSTAL PH 4.6. CRYSTALLIZATION TEMPERATURE 20 C DIFFRACTION TEMPERATURE-160 C'''<br />
 ==Overview==
-BACKGROUND: The folding of the bacterial protease subtilisin BPN' (SBT) is, dependent on its 77-residue prosegment, which is then autocatalytically, removed to give the mature enzyme. Mature subtilisin represents a class of, proteins that lacks an efficient folding pathway. Refolding of mature SBT, is extremely slow unless catalyzed by the independently expressed, prosegment, leading to a bimolecular complex. RESULTS: We report the, crystal structure at 2.0 A resolution of the prosegment-SBT complex and, consider its implications for prosubtilisin BPN' maturation and folding, catalysis. The prosegment forms a compact domain that binds SBT through an, extensive interface involving the enzyme's two parallel surface helices, (residues 104-116 and 133-144), supplying negatively charged caps to the N, termini of these helices. The prosegment C terminus binds in the enzyme, active site in a product-like manner, with Tyr77 in the P1 binding pocket., CONCLUSIONS: The structure of the complex supports a unimolecular, mechanism for prosubtilisin cleavage, involving a 25 A rearrangement of, the SBT N terminus in a late folding step. A mechanism of folding, catalysis in which the two helices and their connecting beta strand form a, prosegment-stabilized folding nucleus is proposed. While this putative, nucleus is stabilized by prosegment binding, the N-terminal and C-terminal, subdomains of SBT could fold by propagation.
+BACKGROUND: The folding of the bacterial protease subtilisin BPN' (SBT) is dependent on its 77-residue prosegment, which is then autocatalytically removed to give the mature enzyme. Mature subtilisin represents a class of proteins that lacks an efficient folding pathway. Refolding of mature SBT is extremely slow unless catalyzed by the independently expressed prosegment, leading to a bimolecular complex. RESULTS: We report the crystal structure at 2.0 A resolution of the prosegment-SBT complex and consider its implications for prosubtilisin BPN' maturation and folding catalysis. The prosegment forms a compact domain that binds SBT through an extensive interface involving the enzyme's two parallel surface helices (residues 104-116 and 133-144), supplying negatively charged caps to the N termini of these helices. The prosegment C terminus binds in the enzyme active site in a product-like manner, with Tyr77 in the P1 binding pocket. CONCLUSIONS: The structure of the complex supports a unimolecular mechanism for prosubtilisin cleavage, involving a 25 A rearrangement of the SBT N terminus in a late folding step. A mechanism of folding catalysis in which the two helices and their connecting beta strand form a prosegment-stabilized folding nucleus is proposed. While this putative nucleus is stabilized by prosegment binding, the N-terminal and C-terminal subdomains of SBT could fold by propagation.
 ==About this Structure==
-SPB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] with NA 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=1SPB OCA].
+SPB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] with <scene name='pdbligand=NA:'>NA</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=1SPB OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Subtilisin]]
-[[Category: Bryan, P.N.]]
+[[Category: Bryan, P N.]]
-[[Category: Gallagher, D.T.]]
+[[Category: Gallagher, D T.]]
-[[Category: Gilliland, G.L.]]
+[[Category: Gilliland, G L.]]
 [[Category: Wang, L.]]
 [[Category: NA]]
@@ Line 24: / Line 24: @@
 [[Category: propeptide]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:32:37 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:03:51 2008''