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1t6p

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[[Image:1t6p.gif|left|200px]]
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{{STRUCTURE_1t6p| PDB=1t6p | SCENE= }}
{{STRUCTURE_1t6p| PDB=1t6p | SCENE= }}
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'''Crystal Structure of Phenylalanine Ammonia Lyase from Rhodosporidium toruloides'''
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===Crystal Structure of Phenylalanine Ammonia Lyase from Rhodosporidium toruloides===
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==Overview==
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The first three-dimensional structure of phenylalanine ammonia lyase (PAL) has been determined at 2.1 A resolution for PAL from Rhodosporidium toruloides. The enzyme is structurally similar to the mechanistically related histidine ammonia lyase (HAL), with PAL having an additional approximately 160 residues extending from the common fold. We propose that catalysis (including lowering the pK(a) of nonacidic C3 of l-phenylalanine for an E1cb mechanism) is potentially governed by dipole moments of seven alpha helices associated with the PAL active site (six positive poles and one negative pole). Cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) resides atop the positive poles of three helices, for increasing its electrophilicity. The helix dipoles appear fully compatible with a model of phenylalanine docked in the active site of PAL having the first covalent bond formed between the amino group of substrate and the methylidene group of MIO: 12 highly conserved residues (near the N termini of helices for enhancing function) are poised to serve roles in substrate recognition, MIO activation, product separation, proton donation, or polarizing electrons from the phenyl ring of substrate for activation of C3; and a highly conserved His residue (near the C terminus of the one helix that directs its negative pole toward the active site to increase the residue's basicity) is positioned to act as a general base, abstracting the pro-S hydrogen from C3 of substrate. A similar mechanism is proposed for HAL, which has a similar disposition of seven alpha helices and similar active-site residues. The helix dipoles appear incompatible with a proposed mechanism that invokes a carbocation intermediate.
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(as it appears on PubMed at http://www.pubmed.gov), where 15350127 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15350127}}
==About this Structure==
==About this Structure==
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[[Category: Mio]]
[[Category: Mio]]
[[Category: Triple helix coiled coil]]
[[Category: Triple helix coiled coil]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:35:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:51:50 2008''

Revision as of 22:51, 27 July 2008

Image:1t6p.png

Template:STRUCTURE 1t6p

Crystal Structure of Phenylalanine Ammonia Lyase from Rhodosporidium toruloides

Template:ABSTRACT PUBMED 15350127

About this Structure

1T6P is a Single protein structure of sequence from Rhodosporidium toruloides. Full crystallographic information is available from OCA.

Reference

Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis., Calabrese JC, Jordan DB, Boodhoo A, Sariaslani S, Vannelli T, Biochemistry. 2004 Sep 14;43(36):11403-16. PMID:15350127

Page seeded by OCA on Mon Jul 28 01:51:50 2008

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