1ilz
From Proteopedia
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|PDB= 1ilz |SIZE=350|CAPTION= <scene name='initialview01'>1ilz</scene>, resolution 2.5Å | |PDB= 1ilz |SIZE=350|CAPTION= <scene name='initialview01'>1ilz</scene>, resolution 2.5Å | ||
|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= pldA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= pldA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1qd5|1QD5]], [[1qd6|1QD6]], [[1fw2|1FW2]], [[1ild|1ILD]], [[1fw3|1FW3]], [[1im0|1IM0]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ilz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ilz OCA], [http://www.ebi.ac.uk/pdbsum/1ilz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ilz 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: asn ala mutation]] | [[Category: asn ala mutation]] | ||
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[[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 21:21:32 2008'' |
Revision as of 18:21, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | pldA (Escherichia coli) | ||||||
| Activity: | Phospholipase A(1), with EC number 3.1.1.32 | ||||||
| Related: | 1QD5, 1QD6, 1FW2, 1ILD, 1FW3, 1IM0
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 6.1
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
1ILZ 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
Page seeded by OCA on Sun Mar 30 21:21:32 2008
Categories: Escherichia coli | Phospholipase A(1) | Single protein | Dekker, N. | Dijkstra, B W. | Eerde, J H.Van. | Egmond, M R. | Kalk, K H. | Kingma, R L. | Snijder, H J. | Anti-parallel beta barrel | Asn ala mutation | Catalytic triad | Membrane phospholipase | Membrane protein | Serine hydrolase
