1im0
From Proteopedia
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|PDB= 1im0 |SIZE=350|CAPTION= <scene name='initialview01'>1im0</scene>, resolution 2.98Å | |PDB= 1im0 |SIZE=350|CAPTION= <scene name='initialview01'>1im0</scene>, resolution 2.98Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene> | + | |LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Phospholipase_A(1) Phospholipase A(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.32 3.1.1.32] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phospholipase_A(1) Phospholipase A(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.32 3.1.1.32] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1qd5|1QD5]], [[1fw2|1FW2]], [[1qd6|1QD6]], [[1fw3|1FW3]], [[1ild|1ILD]], [[1ilz|1ILZ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1im0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1im0 OCA], [http://www.ebi.ac.uk/pdbsum/1im0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1im0 RCSB]</span> | ||
}} | }} | ||
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[[Category: Kingma, R L.]] | [[Category: Kingma, R L.]] | ||
[[Category: Snijder, H J.]] | [[Category: Snijder, H J.]] | ||
| - | [[Category: BOG]] | ||
| - | [[Category: MPD]] | ||
[[Category: anti-parallel beta barrel]] | [[Category: anti-parallel beta barrel]] | ||
[[Category: catalytic triad]] | [[Category: catalytic triad]] | ||
| Line 38: | Line 39: | ||
[[Category: serine hydrolase]] | [[Category: serine hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:21:35 2008'' |
Revision as of 18:21, 30 March 2008
| |||||||
| , resolution 2.98Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Phospholipase A(1), with EC number 3.1.1.32 | ||||||
| Related: | 1QD5, 1FW2, 1QD6, 1FW3, 1ILD, 1ILZ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT PH 8.3
Overview
Outer membrane phospholipase A (OMPLA) from Escherichia coli is an integral-membrane enzyme with a unique His-Ser-Asn catalytic triad. In serine proteases and serine esterases usually an Asp occurs in the catalytic triad; its role has been the subject of much debate. Here the role of the uncharged asparagine in the active site of OMPLA is investigated by structural characterization of the Asn156Ala mutant. Asparagine 156 is not involved in maintaining the overall active-site configuration and does not contribute significantly to the thermal stability of OMPLA. The active-site histidine retains an active conformation in the mutant notwithstanding the loss of the hydrogen bond to the asparagine side chain. Instead, stabilization of the correct tautomeric form of the histidine can account for the observed decrease in activity of the Asn156Ala mutant.
About this Structure
1IM0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: function of the Asn-His interaction in the catalytic triad., Snijder HJ, Van Eerde JH, Kingma RL, Kalk KH, Dekker N, Egmond MR, Dijkstra BW, Protein Sci. 2001 Oct;10(10):1962-9. PMID:11567087
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