1gbh: Difference between revisions

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[[Image:1gbh.jpg|left|200px]]


{{Structure
==ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID==
|PDB= 1gbh |SIZE=350|CAPTION= <scene name='initialview01'>1gbh</scene>, resolution 2.20&Aring;
<StructureSection load='1gbh' size='340' side='right'caption='[[1gbh]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
<table><tr><td colspan='2'>[[1gbh]] 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=1GBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GBH FirstGlance]. <br>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
|GENE= ALPHA-LYTIC PROTEASE PREPROENZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69 Lysobacter enzymogenes])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BLE:LEUCINE+BORONIC+ACID'>BLE</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=1gbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gbh OCA], [https://pdbe.org/1gbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gbh RCSB], [https://www.ebi.ac.uk/pdbsum/1gbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gbh 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/gb/1gbh_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=1gbh ConSurf].
<div style="clear:both"></div>


'''ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID'''
==See Also==
 
*[[Alpha-lytic protease 3D structures|Alpha-lytic protease 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Gly216 in the active site of the broadly specific MA190 mutant of alpha-lytic protease has been found to be remarkably tolerant of amino acid substitutions. Side-chains as large as Trp can be accommodated within the substrate-binding pocket without abolishing catalysis, and have major effects upon the substrate specificity of the enzyme. Kinetic characterization of eleven enzymatically active mutants against a panel of eight substrates clearly revealed the functional consequences of the substitutions at position 216. To understand better the structural basis for their altered specificity, the GA216 + MA190 and GL216 + MA190 mutants have been crystallized both with and without a representative series of peptide boronic acid transition-state analog inhibitors. An empirical description and non-parametric statistical analysis of structural variation among these enzyme: inhibitor complexes is presented. The roles of active site plasticity and dynamics in alpha-lytic protease function and substrate preference are also addressed. The results strongly suggest that substrate specificity determination in alpha-lytic protease is a distributed property of the active site and substrate molecule.
[[Category: Large Structures]]
 
==About this Structure==
1GBH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBH OCA].
 
==Reference==
Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity., Mace JE, Agard DA, J Mol Biol. 1995 Dec 8;254(4):720-36. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7500345 7500345]
[[Category: Alpha-lytic endopeptidase]]
[[Category: Lysobacter enzymogenes]]
[[Category: Lysobacter enzymogenes]]
[[Category: Single protein]]
[[Category: Agard DA]]
[[Category: Agard, D A.]]
[[Category: Mace JE]]
[[Category: Mace, J E.]]
[[Category: SO4]]
[[Category: active-site mutation]]
[[Category: inhibitor complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:20:58 2008''

Latest revision as of 14:20, 27 March 2024

ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACIDALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID

Structural highlights

1gbh is a 2 chain structure with sequence from Lysobacter enzymogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PRLA_LYSEN

Evolutionary Conservation

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

See Also

1gbh, resolution 2.20Å

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