1gnv

From Proteopedia

(Difference between revisions)

Revision as of 10:11, 10 September 2015

CALCIUM INDEPENDENT SUBTILISIN BPN' MUTANT

Structural highlights

1gnv is a 1 chain structure with sequence from "bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1a2q, 1ak9, 1aqn, 1au9, 1s01, 1gns, 1s02, 1sbh, 1sbi, 1sbn, 1sbt, 1sib, 1spb, 1st2, 1sua, 1sub, 1suc, 1sud, 1sue, 1sup, 1ubn, 1yja, 1yjb, 1yjc, 2sbt, 2sic, 2sni, 2st1, 3sic, 5sic
Activity:	Subtilisin, with EC number 3.4.21.62
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[SUBT_BACAM] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structures of two thermally stabilized subtilisin BPN' variants, S63 and S88, are reported here at 1.8 and 1.9 A resolution, respectively. The micromolar affinity calcium binding site (site A) has been deleted (Delta75-83) in these variants, enabling the activity and thermostability measurements in chelating conditions. Each of the variants includes mutations known previously to increase the thermostability of calcium-independent subtilisin in addition to new stabilizing mutations. S63 has eight amino acid replacements: D41A, M50F, A73L, Q206W, Y217K, N218S, S221C, and Q271E. S63 has 75-fold greater stability than wild type subtilisin in chelating conditions (10 mm EDTA). The other variant, S88, has ten site-specific changes: Q2K, S3C, P5S, K43N, M50F, A73L, Q206C, Y217K, N218S, and Q271E. The two new cysteines form a disulfide bond, and S88 has 1000 times greater stability than wild type subtilisin in chelating conditions. Comparisons of the two new crystal structures (S63 in space group P2(1) with A cell constants 41.2, 78.1, 36.7, and beta = 114.6 degrees and S88 in space group P2(1)2(1)2(1) with cell constants 54.2, 60.4, and 82.7) with previous structures of subtilisin BPN' reveal that the principal changes are in the N-terminal region. The structural bases of the stabilization effects of the new mutations Q2K, S3C, P5S, D41A, Q206C, and Q206W are generally apparent. The effects are attributed to the new disulfide cross-link and to improved hydrophobic packing, new hydrogen bonds, and other rearrangements in the N-terminal region.

Structural basis of thermostability. Analysis of stabilizing mutations in subtilisin BPN'.,Almog O, Gallagher DT, Ladner JE, Strausberg S, Alexander P, Bryan P, Gilliland GL J Biol Chem. 2002 Jul 26;277(30):27553-8. Epub 2002 May 13. PMID:12011071^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Peng Y, Huang Q, Zhang RH, Zhang YZ. Purification and characterization of a fibrinolytic enzyme produced by Bacillus amyloliquefaciens DC-4 screened from douchi, a traditional Chinese soybean food. Comp Biochem Physiol B Biochem Mol Biol. 2003 Jan;134(1):45-52. PMID:12524032
↑ Almog O, Gallagher DT, Ladner JE, Strausberg S, Alexander P, Bryan P, Gilliland GL. Structural basis of thermostability. Analysis of stabilizing mutations in subtilisin BPN'. J Biol Chem. 2002 Jul 26;277(30):27553-8. Epub 2002 May 13. PMID:12011071 doi:10.1074/jbc.M111777200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gnv"

Categories: Subtilisin | Almog, O | Gilliland, G L | Hydrolase | Serine proteinase

@@ Line 2: / Line 2: @@
 <StructureSection load='1gnv' size='340' side='right' caption='[[1gnv]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1gnv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GNV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GNV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1gnv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GNV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GNV FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MIS:MONOISOPROPYLPHOSPHORYLSERINE'>MIS</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a2q|1a2q]], [[1ak9|1ak9]], [[1aqn|1aqn]], [[1au9|1au9]], [[1s01|1s01]], [[1gns|1gns]], [[1s02|1s02]], [[1sbh|1sbh]], [[1sbi|1sbi]], [[1sbn|1sbn]], [[1sbt|1sbt]], [[1sib|1sib]], [[1spb|1spb]], [[1st2|1st2]], [[1sua|1sua]], [[1sub|1sub]], [[1suc|1suc]], [[1sud|1sud]], [[1sue|1sue]], [[1sup|1sup]], [[1ubn|1ubn]], [[1yja|1yja]], [[1yjb|1yjb]], [[1yjc|1yjc]], [[2sbt|2sbt]], [[2sic|2sic]], [[2sni|2sni]], [[2st1|2st1]], [[3sic|3sic]], [[5sic|5sic]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gnv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gnv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gnv RCSB], [http://www.ebi.ac.uk/pdbsum/1gnv PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gnv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gnv OCA], [http://pdbe.org/1gnv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gnv RCSB], [http://www.ebi.ac.uk/pdbsum/1gnv PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1gnv" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus amyloliquefaciens]]
 [[Category: Subtilisin]]
 [[Category: Almog, O]]

1gnv

From Proteopedia

Revision as of 10:11, 10 September 2015

CALCIUM INDEPENDENT SUBTILISIN BPN' MUTANT

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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