1afh: Difference between revisions

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New page: left|200px<br /><applet load="1afh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1afh" /> '''LIPID TRANSFER PROTEIN FROM MAIZE SEEDLINGS,...
 
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[[Image:1afh.gif|left|200px]]<br /><applet load="1afh" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1afh" />
'''LIPID TRANSFER PROTEIN FROM MAIZE SEEDLINGS, NMR, 15 STRUCTURES'''<br />


==Overview==
==LIPID TRANSFER PROTEIN FROM MAIZE SEEDLINGS, NMR, 15 STRUCTURES==
The three-dimensional solution structure of a nonspecific lipid transfer, protein extracted from maize seeds determined by 1H NMR spectroscopy is, described. This cationic protein consists of 93 amino acid residues. Its, structure was determined from 1,091 NOE-derived distance restraints, including 929 interresidue connectivities and 197 dihedral restraints, (phi, psi, chi 1) derived from NOEs and 3J coupling constants. The global, fold involving four helical fragments connected by three loops and a, C-terminal tail without regular secondary structures is stabilized by four, disulfide bridges. The most striking feature of this structure is the, existence of an internal hydrophobic cavity running through the whole, molecule. The global fold of this protein, very similar to that of a, previously described lipid transfer protein extracted from wheat seeds, (Gincel E et al., 1994, Eur J Biochem 226:413-422) constitutes a new, architecture for alpha-class proteins. 1H NMR and fluorescence studies, show that this protein forms well-defined complexes in aqueous solution, with lysophosphatidylcholine. Dissociation constants, Kd, of 1.9 +/- 0.6 x, 10(-6) M and &gt; 10(-3) M were obtained with lyso-C16 and -C12, respectively. A structure model for a lipid-protein complex is proposed in, which the aliphatic chain of the phospholipid is inserted in the internal, cavity and the polar head interacts with the charged side chains located, at one end of this cavity. Our model for the lipid-protein complex is, qualitatively very similar to the recently published crystal structure, (Shin DH et al., 1995, Structure 3:189-199).
<StructureSection load='1afh' size='340' side='right'caption='[[1afh]]' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1afh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AFH FirstGlance]. <br>
1AFH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AFH OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1afh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1afh OCA], [https://pdbe.org/1afh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1afh RCSB], [https://www.ebi.ac.uk/pdbsum/1afh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1afh ProSAT]</span></td></tr>
==Reference==
</table>
Solution structure and lipid binding of a nonspecific lipid transfer protein extracted from maize seeds., Gomar J, Petit MC, Sodano P, Sy D, Marion D, Kader JC, Vovelle F, Ptak M, Protein Sci. 1996 Apr;5(4):565-77. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8845747 8845747]
== Function ==
[[Category: Single protein]]
[https://www.uniprot.org/uniprot/NLTP_MAIZE NLTP_MAIZE] Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.
== 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/af/1afh_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=1afh ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Zea mays]]
[[Category: Zea mays]]
[[Category: Gomar, J.]]
[[Category: Gomar J]]
[[Category: Kader, J.C.]]
[[Category: Kader JC]]
[[Category: Marion, D.]]
[[Category: Marion D]]
[[Category: Petit, M.C.]]
[[Category: Petit MC]]
[[Category: Ptak, M.]]
[[Category: Ptak M]]
[[Category: Sodano, P.]]
[[Category: Sodano P]]
[[Category: Sy, D.]]
[[Category: Sy D]]
[[Category: Vovelle, F.]]
[[Category: Vovelle F]]
[[Category: lipid transfer protein]]
[[Category: lipid-binding protein]]
[[Category: maize]]
[[Category: molecular modeling]]
[[Category: nmr]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:48:55 2007''

Latest revision as of 18:23, 13 March 2024

LIPID TRANSFER PROTEIN FROM MAIZE SEEDLINGS, NMR, 15 STRUCTURESLIPID TRANSFER PROTEIN FROM MAIZE SEEDLINGS, NMR, 15 STRUCTURES

Structural highlights

1afh is a 1 chain structure with sequence from Zea mays. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NLTP_MAIZE Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.

Evolutionary Conservation

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

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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