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1akl

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Revision as of 15:08, 12 October 2017

ALKALINE PROTEASE FROM PSEUDOMONAS AERUGINOSA IFO3080

Structural highlights

1akl is a 1 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	Serralysin, with EC number 3.4.24.40
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 structure of the unliganded alkaline protease from Pseudomonas aeruginosa IFO3080 has been determined at 2.0 A resolution by the X-ray method. The enzyme consists of N-terminal catalytic and C-terminal beta-helix domains. On structural comparison between the present unliganded enzyme and structurally- known liganded enzyme, some structural changes were observed around the active site. In the unliganded enzyme, Y216 serves as the fifth ligand for the active site zinc ion. On ligand binding, Y216 may move to form a hydrogen-bond with the carbonyl oxygen of the P1 residue of a ligand peptide. D191 in the flexible loop, Y190 to D196, over the active site cleft forms hydrogen-bonds with the backbone atoms of the P1 and P2 residues of the ligand to close the entrance to the cleft. The water molecule which is the fourth ligand for the zinc ion is replaced by the carbonyl oxygen of the P1 residue. These structural changes around the active site may reflect the substrate-binding mode during the enzymatic reaction.

Crystal structure of the unliganded alkaline protease from Pseudomonas aeruginosa IFO3080 and its conformational changes on ligand binding.,Miyatake H, Hata Y, Fujii T, Hamada K, Morihara K, Katsube Y J Biochem. 1995 Sep;118(3):474-9. PMID:8690704^[1]

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

References

↑ Miyatake H, Hata Y, Fujii T, Hamada K, Morihara K, Katsube Y. Crystal structure of the unliganded alkaline protease from Pseudomonas aeruginosa IFO3080 and its conformational changes on ligand binding. J Biochem. 1995 Sep;118(3):474-9. PMID:8690704

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==ALKALINE PROTEASE FROM PSEUDOMONAS AERUGINOSA IFO3080==
 <StructureSection load='1akl' size='340' side='right' caption='[[1akl]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1akl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AKL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AKL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1akl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AKL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AKL FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Serralysin Serralysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.40 3.4.24.40] </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=1akl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1akl OCA], [http://pdbe.org/1akl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1akl RCSB], [http://www.ebi.ac.uk/pdbsum/1akl 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=1akl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1akl OCA], [http://pdbe.org/1akl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1akl RCSB], [http://www.ebi.ac.uk/pdbsum/1akl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1akl ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 30: / Line 31: @@
 __TOC__
 </StructureSection>
-[[Category: Pseudomonas aeruginosa]]
 [[Category: Serralysin]]
 [[Category: Fujii, T]]

1akl

From Proteopedia

Revision as of 15:08, 12 October 2017

ALKALINE PROTEASE FROM PSEUDOMONAS AERUGINOSA IFO3080

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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