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2flj

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[[Image:2flj.gif|left|200px]]
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[[Image:2flj.png|left|200px]]
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{{STRUCTURE_2flj| PDB=2flj | SCENE= }}
{{STRUCTURE_2flj| PDB=2flj | SCENE= }}
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'''Fatty acid binding protein from locust flight muscle in complex with oleate'''
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===Fatty acid binding protein from locust flight muscle in complex with oleate===
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==Overview==
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Intracellular lipid-binding proteins have evolved from a common ancestral gene with the appearance of mitochondrial oxidation, to guarantee, for example, transport of fatty acids through the aqueous cytosol to their site of utilization. The mammalian forms of these lipid carriers are structurally well-characterized and have been categorized, on the basis of sequence similarities and several typical ligand-binding features, into four subfamilies. Only a single complex structure of an invertebrate fatty-acid-binding protein (FABP) has been reported to date, which reveals a unique ligand-binding arrangement yet unknown in vertebrate FABPs. In the present study, the structure of a second invertebrate FABP (locust muscle) complexed with a fatty acid has been determined on the basis of intermolecular NOE connectivities between the protein and the uniformly (13)C-enriched oleate ligand. The resulting ligand conformation, although resembling the closely related mammalian heart- and adipocyte-type FABPs, is characterized by certain binding features that differ significantly from the typical hairpin-turn ligand shapes of the latter forms. This is primarily due to an alanine-to-leucine substitution in locust FABPs that produces a steric hindrance for ligand binding. A comparison with an FABP from tobacco hornworm larvae furthermore demonstrates that certain amino acid substitutions that appear to be specific for invertebrates decidedly influence the binding arrangement inside the protein cavity. Hence, as a result of these evolutionary variations, invertebrate FABPs may display a much greater diversity in intracellular lipid binding than observed for the mammalian transport proteins, thus possibly providing new insights for the design of modified lipid carriers.
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(as it appears on PubMed at http://www.pubmed.gov), where 16700541 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16700541}}
==About this Structure==
==About this Structure==
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2FLJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Locusta_migratoria Locusta migratoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FLJ OCA].
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2FLJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Locusta_migratoria Locusta migratoria]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FLJ OCA].
==Reference==
==Reference==
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[[Category: Invertebrate fabp]]
[[Category: Invertebrate fabp]]
[[Category: Protein-ligand complex]]
[[Category: Protein-ligand complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:02:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:31:08 2008''

Revision as of 12:31, 29 July 2008

Image:2flj.png

Template:STRUCTURE 2flj

Fatty acid binding protein from locust flight muscle in complex with oleate

Template:ABSTRACT PUBMED 16700541

About this Structure

2FLJ is a Single protein structure of sequence from Locusta migratoria. Full experimental information is available from OCA.

Reference

Fatty-acid-binding protein from the flight muscle of Locusta migratoria: evolutionary variations in fatty acid binding., Lucke C, Qiao Y, van Moerkerk HT, Veerkamp JH, Hamilton JA, Biochemistry. 2006 May 23;45(20):6296-305. PMID:16700541

Page seeded by OCA on Tue Jul 29 15:31:08 2008

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