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1eag

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[[Image:1eag.gif|left|200px]]<br /><applet load="1eag" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1eag, resolution 2.1&Aring;" />
 
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'''SECRETED ASPARTIC PROTEINASE (SAP2) FROM CANDIDA ALBICANS COMPLEXED WITH A70450'''<br />
 
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==Overview==
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==Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450==
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BACKGROUND: Infections caused by Candida albicans, a common fungal pathogen of humans, are increasing in incidence, necessitating development of new therapeutic drugs. Secreted aspartic proteinase (SAP) activity is considered an important virulence factor in these infections and might offer a suitable target for drug design. Amongst the various SAP isozymes, the SAP2 gene product is the major form expressed in a number of C. albicans strains. RESULTS: The three-dimensional structures of SAP2 complexed with the tight-binding inhibitor A70450 (a synthetic hexapeptide analogue) and with the general aspartic proteinase inhibitor pepstatin A (a microbial natural product) have been determined to 2.1 A and 3.0 A resolution, respectively. Although the protein structure retains the main features of a typical aspartic proteinase, it also shows some significant differences, due mainly to several sequence insertions and deletions (as revealed by homology modelling), that alter the shape of the binding cleft. There is also considerable variation in the C-terminal structural domain. CONCLUSIONS: The differences in side chains, and in the conformations adopted by the two inhibitors, particularly at their P4, P3 and P'2 positions (using standard notation for protease-inhibitor residues), allows the A70450 structure to complement, more accurately, that of the substrate-binding site of SAP2. Some differences in the binding clefts of other SAP isoenzymes may be deduced from the SAP2 structure.
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<StructureSection load='1eag' size='340' side='right'caption='[[1eag]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1eag]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EAG FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A70:N-ETHYL-N-[(4-METHYLPIPERAZIN-1-YL)CARBONYL]-D-PHENYLALANYL-N-[(1S,2S,4R)-4-(BUTYLCARBAMOYL)-1-(CYCLOHEXYLMETHYL)-2-HYDROXY-5-METHYLHEXYL]-L-NORLEUCINAMIDE'>A70</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eag OCA], [https://pdbe.org/1eag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eag RCSB], [https://www.ebi.ac.uk/pdbsum/1eag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eag ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CARP2_CANAX CARP2_CANAX]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ea/1eag_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1eag ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1EAG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans] with <scene name='pdbligand=ODS:'>ODS</scene> and <scene name='pdbligand=VAS:'>VAS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Candidapepsin Candidapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.24 3.4.23.24] Known structural/functional Site: <scene name='pdbsite=CAT:Catalytic+Site'>CAT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EAG OCA].
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*[[Pepsin|Pepsin]]
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*[[Proteinase 3D structures|Proteinase 3D structures]]
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==Reference==
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__TOC__
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The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors., Cutfield SM, Dodson EJ, Anderson BF, Moody PC, Marshall CJ, Sullivan PA, Cutfield JF, Structure. 1995 Nov 15;3(11):1261-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8591036 8591036]
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</StructureSection>
[[Category: Candida albicans]]
[[Category: Candida albicans]]
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[[Category: Candidapepsin]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Cutfield JF]]
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[[Category: Cutfield, J F.]]
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[[Category: Cutfield SM]]
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[[Category: Cutfield, S M.]]
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[[Category: ODS]]
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[[Category: VAS]]
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[[Category: candida albicans]]
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[[Category: hydrolase (aspartic protease)]]
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[[Category: sap2]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:25:37 2008''
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Current revision

Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450

PDB ID 1eag

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