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.


1p03

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1p03" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p03, resolution 2.15&Aring;" /> '''STRUCTURE ANALYSIS O...)
Current revision (05:52, 17 April 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1p03.gif|left|200px]]<br /><applet load="1p03" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1p03, resolution 2.15&Aring;" />
 
-
'''STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES'''<br />
 
-
==Overview==
+
==STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES==
-
To better understand the structural basis of enzyme specificity, the, structures of complexes formed between alpha-lytic protease, an, extracellular serine protease of Lysobacter enzymogenes, and five, inhibitory peptide boronic acids (R2-boroX, where R2 is, methoxysuccinyl-Ala-Ala-Pro- and boroX is the alpha-aminoboronic acid, analogue of Ala, Val, Ile, Norleu, or Phe) have been studied at high, resolution by X-ray crystallography. The enzyme has primary specificity, for Ala in the P1 position of peptide substrates with catalytic efficiency, decreasing with increasing side-chain volume. Enzyme affinity for, inhibitors with boroVal, boroIle, and boroPhe residues is much higher than, expected on the basis of the catalytic efficiencies of homologous, substrates. Covalent tetrahedral adducts are formed between the, active-site serine and the boronic acid moieties of R2-boroAla, R2-boroVal, R2-boroIle, and R2-boroNorleu. Though R2-boroVal is a slowly bound, inhibitor and R2-boroAla is rapidly bound [Kettner, C. A., Bone, R., Agard, D. A., &amp; Bachovchin, W. W. (1988) Biochemistry 27, 7682-7688], there appear to be no structural differences that could account for slow, binding. The removal from solution of 20% more hydrophobic surface on, binding accounts for the improved affinity of alpha-lytic protease for, R2-boroVal relative to R2-boroAla. The high affinity of the enzyme for, R2-boroIle derives from the selective binding of the L-allo stereoisomer, of the boroIle residue, which can avoid bad steric interactions in the, binding pocket.(ABSTRACT TRUNCATED AT 250 WORDS)
+
<StructureSection load='1p03' size='340' side='right'caption='[[1p03]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1p03]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P03 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B2V:VALINE+BORONIC+ACID'>B2V</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p03 OCA], [https://pdbe.org/1p03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p03 RCSB], [https://www.ebi.ac.uk/pdbsum/1p03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p03 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/PRLA_LYSEN PRLA_LYSEN]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p0/1p03_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=1p03 ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1P03 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P03 OCA].
+
*[[Alpha-lytic protease 3D structures|Alpha-lytic protease 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Structural analysis of specificity: alpha-lytic protease complexes with analogues of reaction intermediates., Bone R, Frank D, Kettner CA, Agard DA, Biochemistry. 1989 Sep 19;28(19):7600-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2611204 2611204]
+
[[Category: Large Structures]]
-
[[Category: Alpha-lytic endopeptidase]]
+
[[Category: Lysobacter enzymogenes]]
-
[[Category: Single protein]]
+
[[Category: Agard DA]]
-
[[Category: Agard, D.A.]]
+
[[Category: Bone R]]
-
[[Category: Bone, R.]]
+
-
[[Category: SO4]]
+
-
[[Category: hydrolase (serine proteinase)]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:20:04 2007''
+

Current revision

STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES

PDB ID 1p03

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p03"
Personal tools