This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1kuh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:03, 3 April 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1kuh.gif|left|200px]]
 
-
{{Structure
+
==ZINC PROTEASE FROM STREPTOMYCES CAESPITOSUS==
-
|PDB= 1kuh |SIZE=350|CAPTION= <scene name='initialview01'>1kuh</scene>, resolution 1.6&Aring;
+
<StructureSection load='1kuh' size='340' side='right'caption='[[1kuh]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-
|SITE= <scene name='pdbsite=ZIN:Zn+Coordination'>ZIN</scene>
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
+
<table><tr><td colspan='2'>[[1kuh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_caespitosus Streptomyces caespitosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KUH FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kuh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kuh OCA], [https://pdbe.org/1kuh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kuh RCSB], [https://www.ebi.ac.uk/pdbsum/1kuh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kuh ProSAT]</span></td></tr>
-
|RELATEDENTRY=
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kuh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kuh OCA], [http://www.ebi.ac.uk/pdbsum/1kuh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kuh RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/SNPA_STRCS SNPA_STRCS] Specifically hydrolyzes the peptide bond at the imino side of aromatic residues.
-
 
+
== Evolutionary Conservation ==
-
'''ZINC PROTEASE FROM STREPTOMYCES CAESPITOSUS'''
+
[[Image:Consurf_key_small.gif|200px|right]]
-
 
+
Check<jmol>
-
 
+
<jmolCheckbox>
-
==Overview==
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ku/1kuh_consurf.spt"</scriptWhenChecked>
-
A zinc endoprotease produced by Streptomyces caespitosus (ScNP) specifically hydrolyzes the peptide bond at the imino side of aromatic residues and is the smallest protease found to date. Although ScNP carries the zinc-binding sequence HEXXH, its primary structure of 132 amino acid residues differs from those of other known zinc metalloendoproteases. X-ray structural analysis of ScNP at 1.6 A resolution revealed that despite a lack of sequence homology, the common topological feature of main-chain folding and a beta-turn containing methionine, which is a feature of the zinc metalloendoprotease superfamily of metzincins, is conserved in ScNP. The zinc atom of ScNP is tetrahedrally ligated by the two histidines in the HEXXH sequence, an aspartate residue and a water molecule. Thus, ScNP represents a novel subfamily of metzincins with a HEXXHXXGXXD zinc-binding sequence. A plausible substrate recognition pocket to which aromatic residues bind is located near the catalytic zinc ion.
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
 
+
<text>to colour the structure by Evolutionary Conservation</text>
-
==About this Structure==
+
</jmolCheckbox>
-
1KUH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_caespitosus Streptomyces caespitosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KUH OCA].
+
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kuh ConSurf].
-
 
+
<div style="clear:both"></div>
-
==Reference==
+
__TOC__
-
Structure of the zinc endoprotease from Streptomyces caespitosus., Kurisu G, Kinoshita T, Sugimoto A, Nagara A, Kai Y, Kasai N, Harada S, J Biochem. 1997 Feb;121(2):304-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9089404 9089404]
+
</StructureSection>
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
[[Category: Streptomyces caespitosus]]
[[Category: Streptomyces caespitosus]]
-
[[Category: Harada, S.]]
+
[[Category: Harada S]]
-
[[Category: Kai, Y.]]
+
[[Category: Kai Y]]
-
[[Category: Kasai, N.]]
+
[[Category: Kasai N]]
-
[[Category: Kinoshita, T.]]
+
[[Category: Kinoshita T]]
-
[[Category: Kurisu, G.]]
+
[[Category: Kurisu G]]
-
[[Category: Nagara, A.]]
+
[[Category: Nagara A]]
-
[[Category: Sugimoto, A.]]
+
[[Category: Sugimoto A]]
-
[[Category: hydrolase]]
+
-
[[Category: metalloproteinase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:53:40 2008''
+

Current revision

ZINC PROTEASE FROM STREPTOMYCES CAESPITOSUS

PDB ID 1kuh

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools